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4x2x

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'''Unreleased structure'''
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==Crystal structure of the Murine Norovirus NS6 protease (inactive C139A mutant) with a C-terminal extension to include residues P1 prime - P4 prime of NS7==
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<StructureSection load='4x2x' size='340' side='right' caption='[[4x2x]], [[Resolution|resolution]] 2.47&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4x2x]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X2X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4X2X FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ash|4ash]], [[4x2v|4x2v]], [[4x2w|4x2w]]</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4x2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x2x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4x2x RCSB], [http://www.ebi.ac.uk/pdbsum/4x2x PDBsum]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Murine noroviruses have emerged as a valuable tool for investigating the molecular basis of infection and pathogenesis of the closely related human noroviruses, which are the major cause of non-bacterial gastroenteritis. The replication of noroviruses relies on the proteolytic processing of a large polyprotein precursor into six non-structural proteins (NS1-2, NS3, NS4, NS5, NS6(pro), NS7(pol)) by the virally-encoded NS6 protease. We report here the crystal structure of MNV NS6(pro), which has been determined to a resolution of 1.6 A. Adventitiously, the crystal contacts are mediated in part by the binding of the C-terminus of NS6(pro) within the peptide-binding cleft of a neighbouring molecule. This insertion occurs for both molecules in the asymmetric unit of the crystal in a manner that is consistent with physiologically-relevant binding, thereby providing two independent views of a protease-peptide complex. Since the NS6(pro) C-terminus is formed in vivo by NS6(pro) processing, these crystal contacts replicate the protease-product complex that is formed immediately following cleavage of the peptide bond at the NS6-NS7 junction. The observed mode of binding of the C-terminal product peptide yields new insights into the structural basis of NS6(pro) specificity.
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The entry 4x2x is ON HOLD until Paper Publication
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Structure of a Murine Norovirus NS6 Protease-Product Complex Revealed by Adventitious Crystallisation.,Leen EN, Baeza G, Curry S PLoS One. 2012;7(6):e38723. Epub 2012 Jun 7. PMID:22685603<ref>PMID:22685603</ref>
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Authors: Leen, E.N., Cromwell Jr, H., Fernandes, H., Curry, S.
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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Description: Crystal structure of the Murine Norovirus NS6 protease (inactive C139A mutant) with a C-terminal extension to include residues P1 prime -P4 prime of NS7
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== References ==
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[[Category: Unreleased Structures]]
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<references/>
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[[Category: Leen, E.N]]
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__TOC__
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</StructureSection>
[[Category: Curry, S]]
[[Category: Curry, S]]
[[Category: Fernandes, H]]
[[Category: Fernandes, H]]
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[[Category: Cromwell Jr, H]]
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[[Category: Jr, H Cromwell]]
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[[Category: Leen, E N]]
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[[Category: Murine norovirus protease]]
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[[Category: Viral protein]]

Revision as of 12:58, 18 February 2015

Crystal structure of the Murine Norovirus NS6 protease (inactive C139A mutant) with a C-terminal extension to include residues P1 prime - P4 prime of NS7

4x2x, resolution 2.47Å

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