2duc

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==Crystal structure of SARS coronavirus main proteinase(3CLPRO)==
==Crystal structure of SARS coronavirus main proteinase(3CLPRO)==
<StructureSection load='2duc' size='340' side='right' caption='[[2duc]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='2duc' size='340' side='right' caption='[[2duc]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2duc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cvhsa Cvhsa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DUC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DUC FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2duc]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DUC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DUC FirstGlance]. <br>
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</td></tr><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=2duc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2duc OCA], [http://pdbe.org/2duc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2duc RCSB], [http://www.ebi.ac.uk/pdbsum/2duc PDBsum], [http://www.topsan.org/Proteins/RSGI/2duc TOPSAN]</span></td></tr>
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</td></tr><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=2duc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2duc OCA], [http://pdbe.org/2duc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2duc RCSB], [http://www.ebi.ac.uk/pdbsum/2duc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2duc ProSAT], [http://www.topsan.org/Proteins/RSGI/2duc TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2duc ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The 3C-like protease (3CLpro) of severe acute respiratory syndrome coronavirus (SARS-CoV) cleaves 11 sites in the polyproteins, including its own N- and C-terminal autoprocessing sites, by recognizing P4-P1 and P1'. In this study, we determined the crystal structure of 3CLpro with the C-terminal prosequence and the catalytic-site C145A mutation, in which the enzyme binds the C-terminal prosequence of another molecule. Surprisingly, Phe at the P3' position [Phe(P3')] is snugly accommodated in the S3' pocket. Mutations of Phe(P3') impaired the C-terminal autoprocessing, but did not affect N-terminal autoprocessing. This difference was ascribed to the P2 residue, Phe(P2) and Leu(P2), in the C- and N-terminal sites, as follows. The S3' subsite is formed by Phe(P2)-induced conformational changes of 3CLpro and the direct involvement of Phe(P2) itself. In contrast, the N-terminal prosequence with Leu(P2) does not cause such conformational changes for the S3' subsite formation. In fact, the mutation of Phe(P2) to Leu in the C-terminal autoprocessing site abolishes the dependence on Phe(P3'). These mechanisms explain why Phe is required at the P3' position when the P2 position is occupied by Phe rather than Leu, which reveals a type of subsite cooperativity. Moreover, the peptide consisting of P4-P1 with Leu(P2) inhibits protease activity, whereas that with Phe(P2) exhibits a much smaller inhibitory effect, because Phe(P3') is missing. Thus, this subsite cooperativity likely exists to avoid the autoinhibition of the enzyme by its mature C-terminal sequence, and to retain the efficient C-terminal autoprocessing by the use of Phe(P2).
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SARS-CoV 3CL protease cleaves its C-terminal autoprocessing site by novel subsite cooperativity.,Muramatsu T, Takemoto C, Kim YT, Wang H, Nishii W, Terada T, Shirouzu M, Yokoyama S Proc Natl Acad Sci U S A. 2016 Nov 15;113(46):12997-13002. Epub 2016 Oct 31. PMID:27799534<ref>PMID:27799534</ref>
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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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<div class="pdbe-citations 2duc" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Cvhsa]]
 
[[Category: Kim, Y T]]
[[Category: Kim, Y T]]
[[Category: Muramatsu, T]]
[[Category: Muramatsu, T]]

Revision as of 06:08, 17 August 2017

Crystal structure of SARS coronavirus main proteinase(3CLPRO)

2duc, resolution 1.70Å

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