5tsn | pdb_00005tsn

Crystal structures of Norwalk virus polymerase bound to an RNA primer-template duplex

spinqualitylabelsall models 5tsn, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5tsn is a 3 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Norovirus (NV) RNA-dependent RNA polymerase (RdRP) is essential for replicating the genome of the virus, which makes this enzyme a key target for the development of antiviral agents against NV gastroenteritis. In this work, a complex of NV RdRP bound to manganese ions and an RNA primer-template duplex was investigated using X-ray crystallography and hybrid quantum chemical/molecular mechanical simulations. Experimentally, the complex crystallized in a tetragonal crystal form. The nature of the primer/template duplex binding in the resulting structure indicates that the complex is a closed back-tracked state of the enzyme, in which the 3'-end of the primer occupies the position expected for the post-incorporated nucleotide before translocation. Computationally, it is found that the complex can accept a range of divalent metal cations without marked distortions in the active site structure. The highest binding energy is for copper, followed closely by manganese and iron, and then by zinc, nickel and cobalt. This article is protected by copyright. All rights reserved. Norovirus RNA-dependent RNA polymerase: A computational study of metal-binding preferences.,Shaik MM, Bhattacharjee N, Feliks M, Ng KK, Field MJ Proteins. 2017 Apr 6. doi: 10.1002/prot.25304. PMID:28383118 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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