5hm2: Difference between revisions
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==Crystal structure of the 3C protease from South African Territories type 2 foot-and-mouth disease virus== | ==Crystal structure of the 3C protease from South African Territories type 2 foot-and-mouth disease virus== | ||
<StructureSection load='5hm2' size='340' side='right' caption='[[5hm2]], [[Resolution|resolution]] 3.20Å' scene=''> | <StructureSection load='5hm2' size='340' side='right'caption='[[5hm2]], [[Resolution|resolution]] 3.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5hm2]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HM2 OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[5hm2]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Aphthovirus_sat2 Aphthovirus sat2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HM2 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5HM2 FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">3C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=35292 Aphthovirus SAT2])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5hm2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hm2 OCA], [http://pdbe.org/5hm2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hm2 RCSB], [http://www.ebi.ac.uk/pdbsum/5hm2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hm2 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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</div> | </div> | ||
<div class="pdbe-citations 5hm2" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5hm2" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Virus proteases 3D strutures|Virus proteases 3D strutures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Aphthovirus sat2]] | |||
[[Category: Large Structures]] | |||
[[Category: Curry, S]] | [[Category: Curry, S]] | ||
[[Category: Leen, E N]] | [[Category: Leen, E N]] |
Revision as of 11:22, 27 May 2020
Crystal structure of the 3C protease from South African Territories type 2 foot-and-mouth disease virusCrystal structure of the 3C protease from South African Territories type 2 foot-and-mouth disease virus
Structural highlights
Publication Abstract from PubMedThe replication of foot-and-mouth disease virus (FMDV) is dependent on the virus-encoded 3C protease (3C(pro)). As in other picornaviruses, 3C(pro) performs most of the proteolytic processing of the polyprotein expressed from the large open reading frame in the RNA genome of the virus. Previous work revealed that the 3C(pro) from serotype A-one of the seven serotypes of FMDV-adopts a trypsin-like fold. On the basis of capsid sequence comparisons the FMDV serotypes are grouped into two phylogenetic clusters, with O, A, C, and Asia 1 in one, and the three Southern African Territories serotypes, (SAT-1, SAT-2 and SAT-3) in another, a grouping pattern that is broadly, but not rigidly, reflected in 3C(pro) amino acid sequences. We report here the cloning, expression and purification of 3C proteases from four SAT serotype viruses (SAT2/GHA/8/91, SAT1/NIG/5/81, SAT1/UGA/1/97, and SAT2/ZIM/7/83) and the crystal structure at 3.2 A resolution of 3C(pro) from SAT2/GHA/8/91. Crystal structure of the 3C protease from Southern African Territories type 2 foot-and-mouth disease virus.,Yang J, Leen EN, Maree FF, Curry S PeerJ. 2016 Apr 26;4:e1964. doi: 10.7717/peerj.1964. eCollection 2016. PMID:27168976[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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