1MBM
NSP4 proteinase from Equine Arteritis Virus
Summary for 1MBM
| Entry DOI | 10.2210/pdb1mbm/pdb |
| Related | 1CQQ 1HAV 1HPG 1L1N |
| Descriptor | chymotrypsin-like serine protease (2 entities in total) |
| Functional Keywords | serine proteinase, chymotrypsin-like proteinase, collapsed oxyanion hole, transferase |
| Biological source | Equine arteritis virus |
| Cellular location | 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 |
| Total number of polymer chains | 4 |
| Total formula weight | 81510.80 |
| Authors | 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. (deposition date: 2002-08-03, release date: 2002-10-23, Last modification date: 2024-02-14) |
| Primary citation | 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 Cited by 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: 12163505DOI: 10.1074/jbc.M206978200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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