1mbm: Difference between revisions
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'''NSP4 proteinase from Equine Arteritis Virus''' | {{Structure | ||
|PDB= 1mbm |SIZE=350|CAPTION= <scene name='initialview01'>1mbm</scene>, resolution 2.00Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= NSP4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11047 Equine arteritis virus]) | |||
}} | |||
'''NSP4 proteinase from Equine Arteritis Virus''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1MBM is a [ | 1MBM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Equine_arteritis_virus Equine arteritis virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MBM OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12163505 12163505] | ||
[[Category: Equine arteritis virus]] | [[Category: Equine arteritis virus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: serine proteinase]] | [[Category: serine proteinase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:41:29 2008'' | ||
Revision as of 10:41, 20 March 2008
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| 1mbm, resolution 2.00Å | |||||||||||||
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| Gene: | NSP4 (Equine arteritis virus) | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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
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