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Protein Dynamics, Folding, and Allostery II

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Protein Dynamics, Folding, and Allostery II 544a Wednesday, February 21, 2018 Symposium: Transmembrane Signals and 2692-Symp Serial Femtosecond Crystallography of G Protein-Coupled Receptors Signaling Mechanisms Vadim Cherezov. University of Southern California, Los Angeles, CA, USA. 2689-Symp G Protein-Coupled Receptors (GPCRs) are versatile cellular gatekeepers Structure and Dynamics of Functional Chemotaxis Receptor Nanoarrays that regulate a variety of physiological processes in the human body and by NMR and Hydrogen Exchange have been targeted by a large share of pharmaceutical drugs. Structural Maryam Kashefi, Xuni Li, Elizabeth R. Haglin, Lynmarie K. Thompson. studies of this superfamily have been enabled a decade ago by multiple Chemistry, University of Massachusetts, Amherst, MA, USA. breakthroughs in technology that included receptor stabilization, crystalliza- Chemotaxis receptors bind ligands from outside the cell and transmit signals tion in a membrane environment, and microcrystallography. The recent across the membrane to direct the swimming of bacteria towards favorable emergence of X-ray free electron lasers (XFELs) has further accelerated environments. The signaling mechanism is thought to involve a 2 A˚ piston structural studies of GPCRs and other challenging macromolecules by over- displacement of an alpha helix that extends through the periplasmic and coming radiation damage and providing access to high-resolution room tem- transmembrane domains. However, it is not known how the signal then perature structures and dynamics using micrometer-sized crystals. This talk propagates an additional 200 A˚ through the cytoplasmic domain to control will summarize key technology advancements and major milestones of a kinase bound at the membrane-distal tip of the receptor. To investigate this GPCR research at XFELs, and provide a brief outlook on future develop- process, we prepare functional complexes of the aspartate receptor cyto- ments in the field. plasmic fragment with the kinase CheA and a coupling protein CheW that form extended, hexagonal arrays similar to those found in the cell. The re- ceptors in these native-like nanoarrays exhibit surprising dynamic proper- Symposium: Protein Dynamics, Folding, and ties. Mobility-filtered solid-state NMR experiments have identified a Allostery II: Dynamics and Function highly mobile region on the N terminal side of the methylation domain of the receptor, which is involved in adaptation. Mass spectrometry experi- 2693-Symp ments have revealed slow hydrogen exchange in the protein interaction Structure and Dynamics of the CheY Response Regulators from domain of the receptor, at the binding sites for CheA and CheW, and un- Rhodobacter sphaeroides usual EX1 hydrogen exchange throughout the receptor. Comparison of these Lorena Varela, Matt Smith, Lukas Stelzl, Christian Bell, Judith Armitage, properties in the kinase-on and kinase-off signaling states is being used to Christina Redfield. test and further develop models for the role of dynamics in signal propaga- Dept. of Biochemistry, University of Oxford, United Kingdom, Oxford, tion through the chemoreceptor cytoplasmic domain. This research sup- United Kingdom. ported by NIH grant GM120195. The chemotaxis signalling network of E. coli. depends on autophosphorylation of a histidine protein kinase (HPK) in response to a signal from a sensor 2690-Symp domain, with subsequent transfer of the phosphoryl group to an aspartate on Tuning the Signaling Output of Protein Kinase C response regulator (RR) proteins that bind to the flagellar motor and alter its Alexandra C. Newton. rotation. CheY is a 14kDa single domain RR that is conserved across motile University of California, San Diego, La Jolla, CA, USA. species. It is formed by 5 a-helices and 5 b-strands surrounding a conserved Protein kinase C (PKC) transduces the plethora of signals resulting phosphoryl accepting aspartate residue, and once phosphorylated diffuses to from lipid hydrolysis. Precise control of the amplitude of its signaling the flagellar motor, binding to its FliM component to cause switching of rota- output is essential for cellular homeostasis, and disruption of this control tional direction. The photosynthetic bacterium Rhodobacter sphaeroides has leads to pathophysiologies such as cancer or degenerative diseases. multiple chemosensory pathways formed by homologues of the E. coli chemo- Key to the regulation of the signaling output of most PKC isozymes is sensory proteins. It has six CheY homologues with different effects on chemo- the ability of the cytosolic enzyme to respond to the membrane-embedded taxis. Only CheY6 is able to stop the flagellar motor but either CheY3 or CheY4 lipid second messenger, diacylglycerol, in a dynamic range that prevents are also required for chemotaxis. signaling in the absence of agonists but allows efficient activation in NMR and computational methods have been used to answer questions about the response to small changes in diacylglycerol levels. This contribution de- structure, dynamics and function of two of the CheY’s, CheY3 and CheY6. scribes the regulatory inputs that control the spatiotemporal dynamics of NOEs, chemical shifts and residual dipolar couplings are used to define the PKC signaling. structures of CheY3 and CheY6 in their inactive and active states, where phos- - phorylation is mimicked using BeF3 . We have investigated fast timescale 2691-Symp 1 15 Redox Dependent Trans-Membrane Signaling backbone dynamics using the { H}- N heteronuclear NOE and have used William A. Cramer. CPMG relaxation dispersion experiments to detect low populations of alterna- Biological Sciences, Purdue University, West Lafayette, IN, USA. tive conformations. CheY6 differs from the other R. sphaeroides CheYs and Redox dependent trans-membrane (TM) signaling which activates a kinase E. coli CheY by the insertion of a ten-residue loop before the C-terminal helix. (serine-threonine ‘‘Stt7’’ in the green alga C.reinhardtii) regulates the distribu- We have deleted this loop region from CheY6 in order to determine, using tion of light energy between the two photosystems of oxygenic photosynthesis. in vivo and in vitro assays, if it plays a role in the unique function of CheY6 in R. sphaeroides. Redox reactions mediated by the cytochrome b6f complex (pdb 4OGQ) on the electrochemically positive side of the chloroplast thylakoid membrane activate the kinase on the trans (negative) side, leads to phosphorylation of light- 2694-Symp harvesting chlorophyll proteins and their redistribution between the two photo- Proteostasis Function and Disfunction: The Folding Machines that systems (‘‘state transitions’’). Cloned and expressed Stt7 was characterized in Maintain Proteome Health solution by analytical ultra-centrifugation, electron microscopy, and electro- Judith Frydman. spray mass spectrometry as a 754 residue polypeptide organized as a tetramer Stanford University, Stanford, CA, USA. with MW = 332 kDa having 55% a-helix content, which was active in vitro un- Correct protein folding and quality control are essential for normal cellular der reducing conditions. Physical interaction of b6f and Stt7 is implied by function. The accumulation of misfolded proteins is emerging as central to a perturbation of the secondary structure of Stt7 in the presence of the cyto- wide range of disease states, including many neurodegenerative disorders chrome b6f complex. However, the structure basis for the inference that the such as Huntington’s and Prion Disease. A complex network of molecular trans-membrane signaling is mediated by a trans-membrane (TM) protein chaperones facilitate protein folding and assembly and monitor all aspects of topology is complicated by: (i) the presence of 4 proline residues in the putative protein homeostasis. Chaperones assist the folding of newly translated and Stt7 TM domain, which is unprecedented in the a-helical trans-membrane stress-denatured proteins, as well as affects protein quality control. Our domain of an integral membrane protein, the problem more extreme because research investigates the mechanisms and pathways by which chaperones carry there are 16 Pro residues in the TM domain of tetrameric Stt7; (iii) the inter- out these diverse functions. Systems approaches identified a chaperone network lamellar space is limited in the stacked thylakoids; (iv) utilizing the 2.5 A˚ linked to the protein synthesis apparatus assists protein biogenesis. The emer- crystal structure of the b6f complex (pdb 4OGQ), there is insufficient space gence of this translation-linked chaperone network likely underlies the elabo- for a docking site on the lumen or p-side of the b6f complex. Support: rate co-translational folding process necessary for the evolution of larger NIHGMS-038323 and Henry Koffler Professorship (WAC) and NIHDK- multidomain proteins characteristic of eukaryotic cells. A stress-inducible 063491 (JPW). chaperone network protects cells from environmental stress and assists quality BPJ 8705_8719 Wednesday, February 21, 2018 545a control. These chaperones also communicate with the ubiquitin-proteasome teins, b and g. Notably, in the absence of Ca2þ the g1 subunit promotes large pathway to clear misfolded proteins from the cell. Protein quality control in shifts of the BK conductance-voltage curve towards more negative voltages. the eukaryotic cytosol relies on the sequestration of misfolded cytosolic pro- However, very little is known about how a and g1 subunits interact. In partic- teins in specific quality control compartments. Our studies of chaperone func- ular, what
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