A Framework for Interpreting the Leucine-Rich Repeats of the Listeria Internalins
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Structural Insight Into Marburg Virus Nucleoprotein-RNA Complex Formation
bioRxiv preprint doi: https://doi.org/10.1101/2021.07.13.452116; this version posted July 13, 2021. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. 1 Structural insight into Marburg virus nucleoprotein-RNA complex formation 2 3 Yoko Fujita-Fujiharu1,2,3, Yukihiko Sugita1,2,4, Yuki Takamatsu1,#, Kazuya Houri1,2,3, Manabu 4 Igarashi5, Yukiko Muramoto1,2,3, Masahiro Nakano1,2,3, Yugo Tsunoda1, Stephan Becker6,7, 5 Takeshi Noda1,2,3* 6 7 1 Laboratory of Ultrastructural Virology, Institute for Frontier Life and Medical Sciences, 8 Kyoto University, 53 Shogoin Kawahara-cho, Sakyo-ku, Kyoto 606-8507, Japan 9 2 Laboratory of Ultrastructural Virology, Graduate School of Biostudies, Kyoto University, 53 10 Shogoin Kawahara-cho, Sakyo-ku, Kyoto 606-8507, Japan 11 3 CREST, Japan Science and Technology Agency, 4-1-8 Honcho, Kawaguchi, Saitama 332- 12 0012, Japan 13 4 Hakubi Center for Advanced Research, Kyoto University, Kyoto, Japan. 14 5 Division of Epidemiology, International Institute for Zoonosis Control, Hokkaido University, 15 Sapporo 001-0020, Japan 16 6 Institute of Virology, University of Marburg, 35043 Marburg, Germany. 17 7 German Center for Infection Research (DZIF), Marburg-Gießen-Langen Site, University of 18 Marburg, 35043 Marburg, Germany. 19 20 # present address: Department of Virology I, National Institute of Infectious Diseases, Gakuen 21 4-7-1, Musashimurayama-city, Tokyo 208-0011, Japan 22 *correspondence to: [email protected] 23 24 bioRxiv preprint doi: https://doi.org/10.1101/2021.07.13.452116; this version posted July 13, 2021. -
Α/Β Coiled Coils 2 3 Marcus D
1 α/β Coiled Coils 2 3 Marcus D. Hartmann, Claudia T. Mendler†, Jens Bassler, Ioanna Karamichali, Oswin 4 Ridderbusch‡, Andrei N. Lupas* and Birte Hernandez Alvarez* 5 6 Department of Protein Evolution, Max Planck Institute for Developmental Biology, 72076 7 Tübingen, Germany 8 † present address: Nuklearmedizinische Klinik und Poliklinik, Klinikum rechts der Isar, 9 Technische Universität München, Munich, Germany 10 ‡ present address: Vossius & Partner, Siebertstraße 3, 81675 Munich, Germany 11 12 13 14 * correspondence to A. N. Lupas or B. Hernandez Alvarez: 15 Department of Protein Evolution 16 Max-Planck-Institute for Developmental Biology 17 Spemannstr. 35 18 D-72076 Tübingen 19 Germany 20 Tel. –49 7071 601 356 21 Fax –49 7071 601 349 22 [email protected], [email protected] 23 1 24 Abstract 25 Coiled coils are the best-understood protein fold, as their backbone structure can uniquely be 26 described by parametric equations. This level of understanding has allowed their manipulation 27 in unprecedented detail. They do not seem a likely source of surprises, yet we describe here 28 the unexpected formation of a new type of fiber by the simple insertion of two or six residues 29 into the underlying heptad repeat of a parallel, trimeric coiled coil. These insertions strain the 30 supercoil to the breaking point, causing the local formation of short β-strands, which move the 31 path of the chain by 120° around the trimer axis. The result is an α/β coiled coil, which retains 32 only one backbone hydrogen bond per repeat unit from the parent coiled coil. -
Stapled Peptides—A Useful Improvement for Peptide-Based Drugs
molecules Review Stapled Peptides—A Useful Improvement for Peptide-Based Drugs Mattia Moiola, Misal G. Memeo and Paolo Quadrelli * Department of Chemistry, University of Pavia, Viale Taramelli 12, 27100 Pavia, Italy; [email protected] (M.M.); [email protected] (M.G.M.) * Correspondence: [email protected]; Tel.: +39-0382-987315 Received: 30 July 2019; Accepted: 1 October 2019; Published: 10 October 2019 Abstract: Peptide-based drugs, despite being relegated as niche pharmaceuticals for years, are now capturing more and more attention from the scientific community. The main problem for these kinds of pharmacological compounds was the low degree of cellular uptake, which relegates the application of peptide-drugs to extracellular targets. In recent years, many new techniques have been developed in order to bypass the intrinsic problem of this kind of pharmaceuticals. One of these features is the use of stapled peptides. Stapled peptides consist of peptide chains that bring an external brace that force the peptide structure into an a-helical one. The cross-link is obtained by the linkage of the side chains of opportune-modified amino acids posed at the right distance inside the peptide chain. In this account, we report the main stapling methodologies currently employed or under development and the synthetic pathways involved in the amino acid modifications. Moreover, we report the results of two comparative studies upon different kinds of stapled-peptides, evaluating the properties given from each typology of staple to the target peptide and discussing the best choices for the use of this feature in peptide-drug synthesis. Keywords: stapled peptide; structurally constrained peptide; cellular uptake; helicity; peptide drugs 1. -
The Generic Geometry of Helices and Their Close-Packed Structures
Theor Chem Acc (2010) 125:207–215 DOI 10.1007/s00214-009-0639-4 REGULAR ARTICLE The generic geometry of helices and their close-packed structures Kasper Olsen Æ Jakob Bohr Received: 23 May 2009 / Accepted: 9 September 2009 / Published online: 25 September 2009 Ó The Author(s) 2009. This article is published with open access at Springerlink.com Abstract The formation of helices is an ubiquitous 1 Introduction phenomenon for molecular structures whether they are biological, organic, or inorganic, in nature. Helical struc- Helical structures are common in chain molecules such as tures have geometrical constraints analogous to close- proteins, RNA, and DNA, e.g., a-helices and the A, B and Z packing of three-dimensional crystal structures. For helical forms of DNA. In this paper, we consider the packing of packing the geometrical constraints involve parameters idealized helices formed by a continuous tube with the such as the radius of the helical cylinder, the helical pitch purpose to calculate the constraints on such helices which angle, and the helical tube radius. In this communication, arise from close-packing and space filling considerations; the geometrical constraints for single helix, double helix, we consider single helical tubes, as well as sets of two and for double helices with minor and major grooves are identical helical tubes. It is found that the efficiency of the calculated. The results are compared with values from the use of space depends on the helical pitch angle, and the literature for helical polypeptide backbone structures, the optimum helical pitch angle is determined for single and a-, p-, 310-, and c-helices. -
Breaking Non-Native Hydrophobic Clusters Is the Rate-Limiting Step In
Shibasish Chowdhury Wei Zhang Breaking Non-Native Chun Wu Guoming Xiong Hydrophobic Clusters is the Yong Duan Rate-Limiting Step in the Department of Chemistry and Biochemistry, Folding of an Alanine-Based Center of Biomedical Research Excellence, Peptide University of Delaware, Newark, DE 19716 Received 13 March 2002; accepted 29 April 2002 Abstract: The formation mechanism of an alanine-based peptide has been studied by all-atom molecular dynamics simulations with a recently developed all-atom point-charge force field and the Generalize Born continuum solvent model at an effective salt concentration of 0.2M. Thirty-two simulations were conducted. Each simulation was performed for 100 ns. A surprisingly complex folding process was observed. The development of the helical content can be divided into three phases with time constants of 0.06–0.08, 1.4–2.3, and 12–13 ns, respectively. Helices initiate extreme rapidly in the first phase similar to that estimated from explicit solvent simulations. Hydrophobic collapse also takes place in this phase. A folding intermediate state develops in the second phase and is unfolded to allow the peptide to reach the transition state in the third phase. The folding intermediate states are characterized by the two-turn short helices and the transition states are helix–turn–helix motifs—both of which are stabilized by hydrophobic clusters. The equilibrium helical content, calculated by both the main-chain ⌽–⌿ torsion angles and the main-chain hydrogen bonds, is 64–66%, which is in remarkable agreement with experiments. After corrected for the solvent viscosity effect, an extrapolated folding time of 16–20 ns is obtained that is in qualitative agreement with experiments. -
Structure of Voltage-Modulated Sodium-Selective NALCN-FAM155A Channel Complex ✉ Yunlu Kang 1, Jing-Xiang Wu1,2,3 & Lei Chen 1,2,3
ARTICLE https://doi.org/10.1038/s41467-020-20002-9 OPEN Structure of voltage-modulated sodium-selective NALCN-FAM155A channel complex ✉ Yunlu Kang 1, Jing-Xiang Wu1,2,3 & Lei Chen 1,2,3 Resting membrane potential determines the excitability of the cell and is essential for the cellular electrical activities. The NALCN channel mediates sodium leak currents, which positively adjust resting membrane potential towards depolarization. The NALCN channel is 1234567890():,; involved in several neurological processes and has been implicated in a spectrum of neu- rodevelopmental diseases. Here, we report the cryo-EM structure of rat NALCN and mouse FAM155A complex to 2.7 Å resolution. The structure reveals detailed interactions between NALCN and the extracellular cysteine-rich domain of FAM155A. We find that the non- canonical architecture of NALCN selectivity filter dictates its sodium selectivity and calcium block, and that the asymmetric arrangement of two functional voltage sensors confers the modulation by membrane potential. Moreover, mutations associated with human diseases map to the domain-domain interfaces or the pore domain of NALCN, intuitively suggesting their pathological mechanisms. 1 State Key Laboratory of Membrane Biology, College of Future Technology, Institute of Molecular Medicine, Beijing Key Laboratory of Cardiometabolic Molecular Medicine, Peking University, 100871 Beijing, China. 2 Peking-Tsinghua Center for Life Sciences, Peking University, 100871 Beijing, China. ✉ 3 Academy for Advanced Interdisciplinary Studies, Peking University, 100871 Beijing, China. email: [email protected] NATURE COMMUNICATIONS | (2020) 11:6199 | https://doi.org/10.1038/s41467-020-20002-9 | www.nature.com/naturecommunications 1 ARTICLE NATURE COMMUNICATIONS | https://doi.org/10.1038/s41467-020-20002-9 ALCN channel is a voltage-modulated sodium-selective Therefore, we started with the cryo-EM studies of the NALCN– ion channel1. -
Structural and Biochemical Insights Into the Multiple Functions of Yeast Grx3
Article Structural and Biochemical Insights into the Multiple Functions of Yeast Grx3 Chang-Biao Chi, YaJun Tang, Jiahai Zhang, Ya-Nan Dai, Mohnad Abdalla, Yuxing Chen and Cong-Zhao Zhou School of Life Sciences and Hefei National Laboratory for Physical Sciences at the Microscale, University of Science and Technology of China, Hefei, Anhui 230027, People's Republic of China Key Laboratory of Structural Biology, Chinese Academy of Science, Hefei, Anhui, 230027, People's Republic of China Correspondence to YaJun Tang and Cong-Zhao Zhou: School of Life Sciences and Hefei National Laboratory for Physical Sciences at the Microscale, University of Science and Technology of China, Hefei, Anhui 230027, People's Republic of China. [email protected]; [email protected] https://doi.org/10.1016/j.jmb.2018.02.024 Edited by Charalampo Kalodimos Abstract The yeast Saccharomyces cerevisiae monothiol glutaredoxin Grx3 plays a key role in cellular defense against oxidative stress and more importantly, cooperates with BolA-like iron repressor of activation protein Fra2 to regulate the localization of the iron-sensing transcription factor Aft2. The interplay among Grx3, Fra2 and Aft2 responsible for the regulation of iron homeostasis has not been clearly described. Here we solved the crystal structures of the Trx domain (Grx3Trx) and Grx domain (Grx3Grx) of Grx3 in addition to the solution structure of Fra2. Structural analyses and activity assays indicated that the Trx domain also contributes to the glutathione S-transferase activity of Grx3, via an inter-domain disulfide bond between Cys37 and Cys176. NMR titration and pull-down assays combined with surface plasmon resonance experiments revealed that Fra2 could form a noncovalent heterodimer with Grx3 via an interface between the helix-turn-helix motif of Fra2 and the C- terminal segment of Grx3Grx, different from the previously identified covalent heterodimer mediated by Fe–S cluster. -
Helical Structures Mimicking Chiral Seedpod Opening and Tendril Coiling
sensors Review Helical Structures Mimicking Chiral Seedpod Opening and Tendril Coiling Guangchao Wan † , Congran Jin †, Ian Trase , Shan Zhao and Zi Chen * Thayer School of Engineering, Dartmouth College, Hanover, NH 03755, USA; [email protected] (G.W.); [email protected] (C.J.); [email protected] (I.T.); [email protected] (S.Z.) * Correspondence: [email protected]; Tel.: +1-603-646-6475 † These authors contributed equally to this work. Received: 4 July 2018; Accepted: 3 September 2018; Published: 6 September 2018 Abstract: Helical structures are ubiquitous in natural and engineered systems across multiple length scales. Examples include DNA molecules, plants’ tendrils, sea snails’ shells, and spiral nanoribbons. Although this symmetry-breaking shape has shown excellent performance in elastic springs or propulsion generation in a low-Reynolds-number environment, a general principle to produce a helical structure with programmable geometry regardless of length scales is still in demand. In recent years, inspired by the chiral opening of Bauhinia variegata’s seedpod and the coiling of plant’s tendril, researchers have made significant breakthroughs in synthesizing state-of-the-art 3D helical structures through creating intrinsic curvatures in 2D rod-like or ribbon-like precursors. The intrinsic curvature results from the differential response to a variety of external stimuli of functional materials, such as hydrogels, liquid crystal elastomers, and shape memory polymers. In this review, we give a brief overview of the shape transformation mechanisms of these two plant’s structures and then review recent progress in the fabrication of biomimetic helical structures that are categorized by the stimuli-responsive materials involved. -
Polymeric Impulsive Actuation Mechanisms: Development, Characterization, and Modeling
University of Massachusetts Amherst ScholarWorks@UMass Amherst Doctoral Dissertations Dissertations and Theses October 2019 POLYMERIC IMPULSIVE ACTUATION MECHANISMS: DEVELOPMENT, CHARACTERIZATION, AND MODELING Yongjin Kim University of Massachusetts Amherst Follow this and additional works at: https://scholarworks.umass.edu/dissertations_2 Part of the Applied Mechanics Commons, Condensed Matter Physics Commons, Dynamics and Dynamical Systems Commons, Polymer and Organic Materials Commons, and the Polymer Science Commons Recommended Citation Kim, Yongjin, "POLYMERIC IMPULSIVE ACTUATION MECHANISMS: DEVELOPMENT, CHARACTERIZATION, AND MODELING" (2019). Doctoral Dissertations. 1722. https://doi.org/10.7275/15222926 https://scholarworks.umass.edu/dissertations_2/1722 This Open Access Dissertation is brought to you for free and open access by the Dissertations and Theses at ScholarWorks@UMass Amherst. It has been accepted for inclusion in Doctoral Dissertations by an authorized administrator of ScholarWorks@UMass Amherst. For more information, please contact [email protected]. POLYMERIC IMPULSIVE ACTUATION MECHANISMS: DEVELOPMENT, CHARACTERIZATION, AND MODELING A Dissertation Presented by YONGJIN KIM Submitted to the Graduate School of the University of Massachusetts Amherst in partial fulfillment of the requirements for the degree of DOCTOR OF PHILOSOPHY September 2019 Polymer Science and Engineering © Copyright by Yongjin Kim 2019 All Rights Reserved POLYMERIC IMPULSIVE ACTUATION MECHANISMS: DEVELOPMENT, CHARACTERIZATION, AND MODELING A Dissertation Presented by YONGJIN KIM Approved as to style and content by: ____________________________________ Alfred J. Crosby, Chair ____________________________________ Ryan C. Hayward, Member ____________________________________ Christian D. Santangelo, Member __________________________________ E. Bryan Coughlin, Department Head Polymer Science & Engineering DEDICATION To my family ACKNOWLEDGMENTS First and foremost, I would like to thank my thesis advisor, Professor Al Crosby, for guiding me throughout my Ph.D. -
Uncorrected Proofs
7 METHODS FOR A RAPID AND AUTOMATED DESCRIPTION OF PROTEINS: PROTEIN STRUCTURE, PROTEIN SIMILARITY, AND PROTEIN FOLDING Zhanyong Guo and Dieter Cremer Computational and Theoretical Chemistry Group (CATCO), Department of Chemistry, Southern Methodist University, Dallas, TX, USA INTRODUCTION Protein structure is organized into primary, secondary, tertiary, and quaternary levels expressing in this way its enormous variety and complexity.1–5 There have been numerous attempts of simplifying measured protein structures for the purpose of identifying unique conformational patterns. For example, Venkatachalam6 presented a local description of a protein molecule based merely on the polypeptide chain back- bone. Furthermore, he showed that just two of the three conformational angles (ϕ and ψ) of the backbone have to be specified for a particular amino acid residue because conjugative effects keep the peptide unit planar (the angle ω at the peptide bond is normally close to 180°).6 These simplifications do not hinder the valid description of a protein and confirm earlier predictions1–5 of its periodical structure in agreement with crystallographic data.7 A different approach employed by Kabsch and Sander8 describes secondary struc- tural units (SSUs) in terms of the shape and organization of hydrogen‐bonded units Reviews in Computational Chemistry, Volume 29, First Edition. Edited by Abby L. Parrill and Kenny B. Lipkowitz. © 2016 John Wiley & Sons, Inc. Published 2016 by John Wiley & Sons, Inc. 369 0002644036.INDD 369 12/19/2015 10:10:26 AM 370 METHODS FOR A RAPID AND AUTOMATED DESCRIPTION OF PROTEINS found along the backbone. They were able to identify helices and β‐sheets quickly and precisely. -
Super Secondary Structure Consisting of a Polyproline II Helix and a Β-Turn in Leucine Rich Repeats in Bacterial Type III Secretion System Effectors
The Protein Journal (2018) 37:223–236 https://doi.org/10.1007/s10930-018-9767-9 Super Secondary Structure Consisting of a Polyproline II Helix and a β-Turn in Leucine Rich Repeats in Bacterial Type III Secretion System Effectors Dashdavaa Batkhishig1,2 · Khurelbaatar Bilguun1,3 · Purevjav Enkhbayar1 · Hiroki Miyashita4,5 · Robert H. Kretsinger6 · Norio Matsushima1,5,7 Published online: 12 April 2018 © The Author(s) 2018 Abstract Leucine rich repeats (LRRs) are present in over 100,000 proteins from viruses to eukaryotes. The LRRs are 20–30 residues long and occur in tandem. LRRs form parallel stacks of short β-strands and then assume a super helical arrangement called a solenoid structure. Individual LRRs are separated into highly conserved segment (HCS) with the consensus of LxxLx- LxxNxL and variable segment (VS). Eight classes have been recognized. Bacterial LRRs are short and characterized by two prolines in the VS; the consensus is xxLPxLPxx with Nine residues (N-subtype) and xxLPxxLPxx with Ten residues (T-subtype). Bacterial LRRs are contained in type III secretion system effectors such as YopM, IpaH3/9.8, SspH1/2, and SlrP from bacteria. Some LRRs in decorin, fribromodulin, TLR8/9, and FLRT2/3 from vertebrate also contain the motifs. In order to understand structural features of bacterial LRRs, we performed both secondary structures assignments using four programs—DSSP-PPII, PROSS, SEGNO, and XTLSSTR—and HELFIT analyses (calculating helix axis, pitch, radius, residues per turn, and handedness), based on the atomic coordinates of their crystal structures. The N-subtype VS adopts a left handed polyproline II helix (PPII) with four, five or six residues and a type I β-turn at the C-terminal side. -
Analog Boc-Trp-Ile-Ala-Aib-Ile-Val-Aib-Leu-Aib-Pro-Ome 2H20 (X-Ray Structure Analysis/Hydrogen Bond/Helix Curvature/Ionophore/Membrane Channel) ISABELLA L
Proc. Natl. Acad. Sci. USA Vol. 83, pp. 9284-9288, December 1986 Chemistry Parallel packing of a-helices in crystals of the zervamicin IIA analog Boc-Trp-Ile-Ala-Aib-Ile-Val-Aib-Leu-Aib-Pro-OMe 2H20 (x-ray structure analysis/hydrogen bond/helix curvature/ionophore/membrane channel) ISABELLA L. KARLE*, MUPPALLA SUKUMARt, AND PADMANABHAN BALARAMt *Laboratory for the Structure of Matter, Naval Research Laboratory, Washington, DC 20375-5000; and tMolecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India Contributed by Isabella L. Karle, September 8, 1986 ABSTRACT An apolar synthetic analog of the first 10 crystals were grown from dimethyl sulfoxide/H20 in the residues at the NH2-terminal end of zervamicin HA crystallizes form of triangular prisms. X-ray diffraction data were mea- in the triclinic space group P1 with cell dimensions a = 10.206 + sured from a crystal that was 0.10 mm thick and 0.30 mm on 0.002 A, b = 12.244 + 0.002 A, c = 15.049 ± 0.002 i, a = 93.94 each side of the triangular face. The crystal was sealed in a ± 0.010, /8 = 95.10 ± 0.010, y = 104.56 _ 0.01°, Z = 1, capillary with a small amount ofmother liquor. The data were C6oH97N1103-2H2O. Despitetherelativelyfew a-aminoisobutyric collected with a four-circle automated diffractometer using acid residues, the peptide maintains a helical form. The first Cu Ka radiation and a graphite monochromator (A = 1.54178 intrahelical hydrogen bond is of the 310 type between N(3) and A). The 0-20 scan technique was used with a 2.00 scan, 0(0), followed by five a-helix-type hydrogen bonds.