2B8H

A/NWS/whale/Maine/1/84 (H1N9) reassortant influenza virus neuraminidase

2B8H の概要

• エントリーDOI: 10.2210/pdb2b8h/pdb
• 関連するPDBエントリー: 1a14 1nmb 1nmc 7nn9
• 分子名称: Neuraminidase, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (9 entities in total)
• 機能のキーワード: 6-bladed beta-propeller, hydrolase
• 由来する生物種: Influenza A virus
• 細胞内の位置: Virion membrane (By similarity): P05803
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 186692.07

構造登録者

Smith, B.J.,Platis, D.,Cox, M.M.J.,Huyton, T.,Joosten, R.P.,McKimm-Breschkin, J.L.,Zhang, J.-G.,Luo, C.S.,Lou, M.-Z.,Garrett, T.P.J.,Labrou, N.E. (登録日: 2005-10-07, 公開日: 2006-09-05, 最終更新日: 2024-10-16)

主引用文献

Smith, B.J.,Huyton, T.,Joosten, R.P.,McKimm-Breschkin, J.L.,Zhang, J.G.,Luo, C.S.,Lou, M.Z.,Labrou, N.E.,Garrett, T.P.
Structure of a calcium-deficient form of influenza virus neuraminidase: implications for substrate binding.
Acta Crystallogr.,Sect.D, 62:947-952, 2006

PubMed Abstract: 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.

PubMed: 16929094
DOI: 10.1107/S0907444906020063

実験手法

X-RAY DIFFRACTION (2.2 Å)