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1mbm
From Proteopedia
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'''NSP4 proteinase from Equine Arteritis Virus''' | '''NSP4 proteinase from Equine Arteritis Virus''' | ||
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[[Category: Ng, K K.S.]] | [[Category: Ng, K K.S.]] | ||
[[Category: Snijder, E J.]] | [[Category: Snijder, E J.]] | ||
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| - | [[Category: | + | [[Category: Collapsed oxyanion hole]] |
| - | [[Category: | + | [[Category: Serine proteinase]] |
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Revision as of 21:51, 2 May 2008
NSP4 proteinase from Equine Arteritis Virus
Overview
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.
About this Structure
1MBM is a Single protein structure of sequence from Equine arteritis virus. Full crystallographic information is available from OCA.
Reference
Structure of arterivirus nsp4. The smallest chymotrypsin-like proteinase with an alpha/beta C-terminal extension and alternate conformations of the oxyanion hole., Barrette-Ng IH, Ng KK, Mark BL, Van Aken D, Cherney MM, Garen C, Kolodenko Y, Gorbalenya AE, Snijder EJ, James MN, J Biol Chem. 2002 Oct 18;277(42):39960-6. Epub 2002 Aug 5. PMID:12163505 Page seeded by OCA on Sat May 3 00:51:44 2008
