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CALENDAR 3Emm About the PSI SBKB sbkb.org • [email protected] 2012CALENDAR 3emm About the PSI SBKB To present a broader view of structural biology and structural The Protein Structure Initiative Structural Biology ABOUT THIS CALENDAR genomics research, the PSI Structural Biology Knowledgebase Knowledgebase (PSI SBKB, sbkb.org) is a free The 2012 PSI SBKB calendar is composed of selections offers centralized access to the following information from the online resource that enables users to discover from the PSI Featured System and Featured Molecule Protein Structure Initiative and beyond: how amino acid sequences, 3D structures, and series, written and illustrated by David Goodsell (The theoretical models help us understand protein Scripps Research Institute) especially for the SBKB. • biological annotations function. A single search of the SBKB will provide Each month features a space-filling representation, • theoretical models links to 3D protein structures, pre-built theoretical (like the image below) which shows the overall shape • all structures in the Protein Data Bank models, biological annotations, structural and volume of the biomolecule, a ribbon diagram to • protein production protocols genomics target information, protocols, and show how the amino acid sequence folds into the • DNA clones and technologies access to DNA clones. The website offers an easy presented 3D shape, and an explanation of biological • research library way to keep abreast of developments by the PSI and/or biomedical relevance of this protein structure • new research and technical highlights and more generally in the fields of structural for readers of all ages and backgrounds. • news and events calendar biology and structural genomics. The PSI SBKB is a collaboration between the Protein ABOUT THE PSI FEATURED SYSTEM The PSI Featured System (on the homepage at sbkb.org) Structure Initiative (PSI) and Nature Publishing is a monthly article about one of the many protein Group (NPG). Funding is provided by the National systems studied by the PSI high-throughput structural Institute of General Medical Sciences. genomics and structural biology efforts. Molecular images are created by the Python Molecular Viewer The Protein Structure Initiative (mgltools.scripps.edu). In addition, the web-version The PSI is a federal, university, and industry effort of the PSI Featured System includes an interactive view to dramatically reduce the costs and reduce the of the protein structure that allows users to explore the time it takes to determine a three-dimensional 3D structure on their own. protein structure. The long-range goal of the PSI is to make the 3D atomic-level structures of most proteins easily obtainable from knowledge of their corresponding DNA sequences. Nature Publishing Group NPG is the scientific publishing arm of Macmillan Publishers Ltd. It publishes journals and online databases across the life, physical and applied sciences and, most recently, clinical medicine. Content encompasses daily news from award- winning journalists, expert opinion, practical methodology, and high impact research and reviews. sbkb.org [email protected] AboutNitrobindin this calendar doi:10.3942/psi_sbkb/fm_2010_12 Proteins perform most of the nanoscale tasks inside of cells, but occasionally, they need help from more exotic molecules. For instance, very small molecules like oxygen are difficult to capture, and proteins like hemoglobin use a heme to trap them. Heme is used in many other capacities as well, including the management of electrons and the capture of other gas molecules such as nitric oxide. So, when researchers at CESG discovered a ON THE COVER THE ON new heme-containing protein in the plant Arabidopsis, they were faced with an exciting challenge: what is the heme doing? HEME EXPOSED One clue to the function of nitrobindin is provided The heme in nitrobindin (PDB entry 3emm, by the similar NO-binding protein nitrophorin. pictured on the cover and at right) is unusual in that Nitrophorin is made by blood-sucking insects and the iron atom found in all heme molecules is rather used to deliver NO to their victims, where it dilates exposed to solvent. In many heme proteins, the the blood vessels and provides more blood for the heme is buried deep within the protein, with per- insect. Nitrobindin may play a similar role in plants, fectly-placed amino acids guarding access to the providing a way to store NO safely until it is needed. iron atom. For instance, globins have a histidine on one side of the heme, which positions the iron in ANOTHER NITROBINDIN the proper place, and a histidine or glutamine on Structural genomics often acts like a snowball, the other side, leaving just enough room for oxygen starting with a central piece of information, then to bind. Nitrobindin, on the other hand, has a sim- growing around that. Building on the Arabidopsis ilar histidine coordinated directly to the iron, but nitrobindin structure, researchers at the CESG then the other side of the iron is free to interact with looked to the human genome and found a similar water. This has an unusual consequence: in the pres- protein there. The protein THAP4 includes a ence of oxygen, the iron atom is rapidly oxidized modified zinc finger, which binds to DNA, as well and shows only a weak interaction with oxygen. as a nitrobindin-style heme-binding domain. A 3emm recent crystallographic structure of the nitrobindin MANAGING NITRIC OXIDE portion (PDB entry 3ia8, not shown) revealed a Testing revealed, however, that the reduced form structure very similar to the Arabidopsis nitrobindin, of the protein binds to nitric oxide (NO) with with a beautifully symmetrical beta barrel, a heme- substantial affinity. This has posed a mystery about binding pocket at one end and a special shape called the function of the protein. Nitric oxide, in spite of a 310 helix at the opposite end. its significant toxicity, is widely used in animal cells SBKB Quick Fact as a hormone in particular, in the local control of blood flow. It plays a similar role in plant cells as The SBKB is updated weekly with new targets, structures, part of a complex signaling network that decides Bianchetti, C. M. et al. Proteins 78, 917- 931 (2010). PDB ID: 3emm methods, and annotations. Learn about all this, and how to Wendehenne, D. et al. Nitric oxide: a new player in plant signalling and defence responses what to do when cells are infected or wounded. Curr. Op. Plant Biol. 7, 449-455 (2004). subscribe to RSS feeds and E-alerts, at sbkb.org The Perils of Protein Secretion doi:10.3942/psi_sbkb/fm_2011_11 Salmonella bacteria are tiny terrorists that infect cells and ultimately destroy them. They don't, however, just kill cells outright. The attack is far more measured, so that the bacteria have time to multiply within the cell before the cell dies. To control this process, Salmonella bacteria inject a deadly cocktail of proteins into their targets. These "effector" proteins assist in the entry of bacteria into the cells, they thwart cellu- lar defense systems, and they ultimately destroy the cells when the bacteria have finished with them. DEADLY NEEDLE hobble the immune system. In other cases, such as Many of these effector proteins are injected into epithelial cells, it needs to wait and kill the cell cells through a "needle complex"through a process later, when it's ready to escape and spread. The known as type III secretion. Structures are available bacterial effector proteins make these decisions, for a few of the many components of this complex, forcing infected cells to die on command. For as shown in the top image. In the image, we are instance, the SlrP protein of Salmonella mimics the looking from the outside of the cell through the E3 ubiquitin ligases. These ligases normally control middle of the complex. At the center, there is a the disposal of obsolete proteins in our cells by "needle" protein with a narrow opening, shown in attaching the small protein ubiquitin to them, red from PDB entry 2v6l. Because the opening is so which marks them for destruction by the protea- small, effector proteins must be unfolded before some. SlrP hijacks this system, using it instead to they are threaded through the hole and into the destroy essential proteins involved in the cellular infected cell. Surrounding the needle several con- immune response. centric rings of proteins, shown here in blue and green from PDB entries 2y9j and 2y9k, that anchor EXPLORING AN EFFECTOR PROTEIN MCSG researchers are exploring the structures of the needle in the bacterial cell wall. 2v6l 2y9j 2y9k these bacterial E3 ubiquitin ligases, looking at the SlrP protein of Salmonella and the similar protein CAREFUL REGULATION 3cvr 3ckd As you can imagine, this process must be carefully IpaH from Shigella. This is a bit tricky because they regulated, so that the proper effector proteins are are flexible proteins, with two separate domains injected at the proper time. Researchers at PCSEP connected by a short hinge, so PSI researchers had are using protein network analysis to uncover the to cut the enzymes into two pieces and solve the many players involved in this control. By looking at structures of each half individually. One half, the proteins that are expressed during infection, shown here on the left from PDB entry 3cvr, and comparing these to the bacterial proteins that recognizes the target protein, and the other half, are expressed at other times, they can identify the shown on the right from PDB entry 3ckd, performs proteins specifically involved in secretion, and the reaction that connects ubiquitin. determine networks of how they interact with one another. By analyzing these networks, they have Deane, J.E. et al. Molecular model of a type III secretion system needle: Implications discovered that many mechanisms come into play, for host-cell sensing.
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