1MBM

NSP4 proteinase from Equine Arteritis Virus

1MBM の概要

• エントリーDOI: 10.2210/pdb1mbm/pdb
• 関連するPDBエントリー: 1CQQ 1HAV 1HPG 1L1N
• 分子名称: chymotrypsin-like serine protease (2 entities in total)
• 機能のキーワード: serine proteinase, chymotrypsin-like proteinase, collapsed oxyanion hole, transferase
• 由来する生物種: Equine arteritis virus
• 細胞内の位置: Nsp1 papain-like cysteine proteinase: Host nucleus. Nsp2 cysteine proteinase: Host membrane ; Multi-pass membrane protein . Non-structural protein 3: Host membrane ; Multi-pass membrane protein . Non-structural protein 5-6-7: Host membrane ; Multi-pass membrane protein . 3C-like serine proteinase: Host cytoplasm . RNA-directed RNA polymerase: Host cytoplasm, host perinuclear region . Helicase: Host cytoplasm, host perinuclear region : P19811
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 81510.80

構造登録者

Barrette-Ng, I.H.,Ng, K.K.-S.,Mark, B.L.,van Aken, D.,Cherney, M.M.,Garen, C.,Kolodenko, Y.,Gorbalenya, A.E.,Snijder, E.J.,James, M.N.G. (登録日: 2002-08-03, 公開日: 2002-10-23, 最終更新日: 2024-02-14)

主引用文献

Barrette-Ng, I.H.,Ng, K.K.-S.,Mark, B.L.,van Aken, D.,Cherney, M.M.,Garen, C.,Kolodenko, Y.,Gorbalenya, A.E.,Snijder, E.J.,James, M.N.G.
Structure of Arterivirus nsp4: the smallest chymotrypsin-like proteinase with an alpha/beta C-terminal extension and alternate conformations of the oxyanion hole
J.Biol.Chem., 277:39960-39966, 2002

PubMed Abstract: Arteriviruses are enveloped, positive-stranded RNA viruses and include pathogens of major economic concern to the swine- and horse-breeding industries. The arterivirus replicase gene encodes two large precursor polyproteins that are processed by the viral main proteinase nonstructural protein 4 (nsp4). The three-dimensional structure of the 21-kDa nsp4 from the arterivirus prototype equine arteritis virus has been determined to 2.0 A resolution. Nsp4 adopts the smallest known chymotrypsin-like fold with a canonical catalytic triad of Ser-120, His-39, and Asp-65, as well as a novel alpha/beta C-terminal extension domain that may play a role in mediating protein-protein interactions. In different copies of nsp4 in the asymmetric unit, the oxyanion hole adopts either a collapsed inactive conformation or the standard active conformation, which may be a novel way of regulating proteolytic activity.

PubMed: 12163505
DOI: 10.1074/jbc.M206978200

実験手法

X-RAY DIFFRACTION (2 Å)