1mbm

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(New page: 200px<br /><applet load="1mbm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mbm, resolution 2.00&Aring;" /> '''NSP4 proteinase from...)
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[[Image:1mbm.jpg|left|200px]]<br /><applet load="1mbm" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1mbm, resolution 2.00&Aring;" />
caption="1mbm, resolution 2.00&Aring;" />
'''NSP4 proteinase from Equine Arteritis Virus'''<br />
'''NSP4 proteinase from Equine Arteritis Virus'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1MBM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equine_arteritis_virus Equine arteritis virus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MBM OCA].
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1MBM is a [http://en.wikipedia.org/wiki/Single_protein 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==
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[[Category: Equine arteritis virus]]
[[Category: Equine arteritis virus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Aken, D.van.]]
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[[Category: Aken, D van.]]
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[[Category: Barrette-Ng, I.H.]]
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[[Category: Barrette-Ng, I H.]]
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[[Category: Cherney, M.M.]]
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[[Category: Cherney, M M.]]
[[Category: Garen, C.]]
[[Category: Garen, C.]]
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[[Category: Gorbalenya, A.E.]]
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[[Category: Gorbalenya, A E.]]
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[[Category: James, M.N.G.]]
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[[Category: James, M N.G.]]
[[Category: Kolodenko, Y.]]
[[Category: Kolodenko, Y.]]
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[[Category: Mark, B.L.]]
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[[Category: Mark, B L.]]
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[[Category: Ng, K.K.S.]]
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[[Category: Ng, K K.S.]]
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[[Category: Snijder, E.J.]]
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[[Category: Snijder, E J.]]
[[Category: chymotrypsin-like proteinase]]
[[Category: chymotrypsin-like proteinase]]
[[Category: collapsed oxyanion hole]]
[[Category: collapsed oxyanion hole]]
[[Category: serine proteinase]]
[[Category: serine proteinase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:18:42 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:53:39 2008''

Revision as of 11:53, 21 February 2008


1mbm, resolution 2.00Å

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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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