2b8h
From Proteopedia
Revision as of 14:35, 21 February 2008
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A/NWS/whale/Maine/1/84 (H1N9) reassortant influenza virus neuraminidase
Overview
The X-ray structure of influenza virus neuraminidase (NA) isolated from whale, subtype N9, has been determined at 2.2 A resolution and contains a tetrameric protein in the asymmetric unit. In structures of NA determined previously, a calcium ion is observed to coordinate amino acids near the substrate-binding site. In three of the NA monomers determined here this calcium is absent, resulting in structural alterations near the substrate-binding site. These changes affect the conformation of residues that participate in several key interactions between the enzyme and substrate and provide at a molecular level the basis of the structural and functional role of calcium in substrate and inhibitor binding. Several sulfate ions were identified in complex with the protein. These are located in the active site, occupying the space reserved for the substrate (sialic acid) carboxylate, and in positions leading away from the substrate-binding site. These sites offer a new opportunity for the design of inhibitors of influenza virus NA.
About this Structure
2B8H is a Single protein structure of sequence from Influenza a virus with , , and as ligands. Active as Exo-alpha-sialidase, with EC number 3.2.1.18 Full crystallographic information is available from OCA.
Reference
Structure of a calcium-deficient form of influenza virus neuraminidase: implications for substrate binding., Smith BJ, Huyton T, Joosten RP, McKimm-Breschkin JL, Zhang JG, Luo CS, Lou MZ, Labrou NE, Garrett TP, Acta Crystallogr D Biol Crystallogr. 2006 Sep;62(Pt 9):947-52. Epub 2006, Aug 19. PMID:16929094
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