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[[Image:1wqs.gif|left|200px]]
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{{STRUCTURE_1wqs|  PDB=1wqs  |  SCENE=  }}
'''Crystal structure of Norovirus 3C-like protease'''


==Crystal structure of Norovirus 3C-like protease==
<StructureSection load='1wqs' size='340' side='right'caption='[[1wqs]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1wqs]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Chiba_virus Chiba virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WQS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WQS FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=TAR:D(-)-TARTARIC+ACID'>TAR</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1wqs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wqs OCA], [https://pdbe.org/1wqs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wqs RCSB], [https://www.ebi.ac.uk/pdbsum/1wqs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wqs ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9DU47_CHIBA Q9DU47_CHIBA]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wq/1wqs_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1wqs ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Norovirus 3C-like proteases are crucial to proteolytic processing of norovirus polyproteins. We determined the crystal structure of the 3C-like protease from Chiba virus, a norovirus, at 2.8-A resolution. An active site including Cys139 and His30 is present, as is a hydrogen bond network that stabilizes the active site conformation. In the oxyanion hole backbone, a structural difference was observed probably upon substrate binding. A peptide substrate/enzyme model shows that several interactions between the two components are critical for substrate binding and that the S1 and S2 sites appropriately accommodate the substrate P1 and P2 residues, respectively. Knowledge of the structure and a previous mutagenesis study allow us to correlate proteolysis and structure.


==Overview==
A norovirus protease structure provides insights into active and substrate binding site integrity.,Nakamura K, Someya Y, Kumasaka T, Ueno G, Yamamoto M, Sato T, Takeda N, Miyamura T, Tanaka N J Virol. 2005 Nov;79(21):13685-93. PMID:16227288<ref>PMID:16227288</ref>
Norovirus 3C-like proteases are crucial to proteolytic processing of norovirus polyproteins. We determined the crystal structure of the 3C-like protease from Chiba virus, a norovirus, at 2.8-A resolution. An active site including Cys139 and His30 is present, as is a hydrogen bond network that stabilizes the active site conformation. In the oxyanion hole backbone, a structural difference was observed probably upon substrate binding. A peptide substrate/enzyme model shows that several interactions between the two components are critical for substrate binding and that the S1 and S2 sites appropriately accommodate the substrate P1 and P2 residues, respectively. Knowledge of the structure and a previous mutagenesis study allow us to correlate proteolysis and structure.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1WQS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Chiba_virus Chiba virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WQS OCA].
</div>
<div class="pdbe-citations 1wqs" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
A norovirus protease structure provides insights into active and substrate binding site integrity., Nakamura K, Someya Y, Kumasaka T, Ueno G, Yamamoto M, Sato T, Takeda N, Miyamura T, Tanaka N, J Virol. 2005 Nov;79(21):13685-93. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16227288 16227288]
*[[Virus protease 3D structures|Virus protease 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Chiba virus]]
[[Category: Chiba virus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Kumasaka, T.]]
[[Category: Kumasaka T]]
[[Category: Nakamura, K.]]
[[Category: Nakamura K]]
[[Category: Someya, Y.]]
[[Category: Someya Y]]
[[Category: Tanaka, N.]]
[[Category: Tanaka N]]
[[Category: 3c-like protease]]
[[Category: Chymotrypsin like protease]]
[[Category: Crystal structure]]
[[Category: Norovirus]]
[[Category: Norwalk-like virus]]
[[Category: Oxyanion hole]]
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