4ash: Difference between revisions
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<StructureSection load='4ash' size='340' side='right'caption='[[4ash]], [[Resolution|resolution]] 1.58Å' scene=''> | <StructureSection load='4ash' size='340' side='right'caption='[[4ash]], [[Resolution|resolution]] 1.58Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ash]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4ash]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Murine_norovirus_1 Murine norovirus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ASH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ASH FirstGlance]. <br> | ||
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Calicivirin Calicivirin], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.66 3.4.22.66] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ash FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ash OCA], [https://pdbe.org/4ash PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ash RCSB], [https://www.ebi.ac.uk/pdbsum/4ash PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ash ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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==See Also== | ==See Also== | ||
*[[ | *[[Virus protease 3D structures|Virus protease 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Calicivirin]] | [[Category: Calicivirin]] | ||
[[Category: Large Structures]] | |||
[[Category: Murine norovirus 1]] | [[Category: Murine norovirus 1]] | ||
[[Category: Baeza, G]] | [[Category: Baeza, G]] | ||
Revision as of 08:44, 25 August 2022
Crystal structure of the NS6 protease from murine norovirus 1Crystal structure of the NS6 protease from murine norovirus 1
Structural highlights
Publication Abstract from PubMedMurine 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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