1s49 | pdb_00001s49

Crystal Structure of RNA-dependent RNA polymerase construct 1 (residues 71-679) from bovine viral diarrhea virus complexed with GTP

spinqualitylabelsall models 1s49, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1s49 is a 1 chain structure with sequence from Bovine viral diarrhea virus 1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GTP NonStd Res: MSE Related: 1s48, 1s4f Gene: NS5B (Bovine viral diarrhea virus 1) Resources: FirstGlance, OCA, RCSB, PDBsum Function [POLG_BVDVN] Initial binding to target cell probably involves interaction of E(rns) with glycosaminoglycans. E1 and/or E2 are responsible of cell attachment with CD46 and subsequent fusion after internalization of the virion by endocytosis (Probable). P7 forms a leader sequence to properly orient NS2 in the membrane (By similarity). Uncleaved NS2-3 is required for production of infectious virus. NS2 protease seems to play a vital role in viral RNA replication control and in the pathogenicity of the virus. NS3 displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS4A is a cofactor for the NS3 protease activity (By similarity). RNA-directed RNA polymerase NS5 replicates the viral (+) and (-) genome. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The bovine viral diarrhea virus (BVDV) RNA-dependent RNA polymerase can initiate RNA replication by a de novo mechanism without a primer. The structure of BVDV polymerase, determined to 2.9-A resolution, contains a unique N-terminal domain, in addition to the fingers, palm, and thumb domains common to other polymerases. The structure of BVDV polymerase complexed with GTP, which is required for de novo (primer-independent) initiation, shows that GTP binds adjacent to the initiation NTP, suggesting that the GTP mimics a vestigial RNA product. Comparison of five monomers in two different crystal forms showed conformational changes in the fingertip region and in the thumb domain that may help to translocate the RNA template and product strands during elongation. The putative binding sites of previously reported BVDV inhibitors are also discussed. The structure of the RNA-dependent RNA polymerase from bovine viral diarrhea virus establishes the role of GTP in de novo initiation.,Choi KH, Groarke JM, Young DC, Kuhn RJ, Smith JL, Pevear DC, Rossmann MG Proc Natl Acad Sci U S A. 2004 Mar 30;101(13):4425-30. Epub 2004 Mar 19. PMID:15070734 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also RNA polymerase

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