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==Crystal Structure of ASFV pS273R protease==
<StructureSection load='6ljb' size='340' side='right'caption='[[6ljb]], [[Resolution|resolution]] 2.49&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6ljb]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Asfk5 Asfk5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LJB OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6LJB FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Ken-123 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=561445 ASFK5])</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=6ljb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ljb OCA], [http://pdbe.org/6ljb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ljb RCSB], [http://www.ebi.ac.uk/pdbsum/6ljb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ljb ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/VPRT_ASFK5 VPRT_ASFK5]] Protease involved in the processing of both viral polyproteins pp220 and pp62. 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
African swine fever (ASF) is a highly contagious hemorrhagic viral disease of domestic and wild pigs that is responsible for serious economic and production losses. It is caused by the African swine fever virus (ASFV), a large and complex icosahedral DNA virus of the Asfarviridae family. Currently, there is no effective treatment or approved vaccine against the ASFV. pS273R, a specific SUMO-1 cysteine protease, catalyzes the maturation of the pp220 and pp62 polyprotein precursors into core-shell proteins. Here, we present the crystal structure of the ASFV pS273R protease at a resolution of 2.3 angstroms. The overall structure of the pS273R protease is represented by two domains named the "core domain" and the N-terminal "arm domain". The "arm domain" contains the residues from M1 to N83, and the "core domain" contains the residues from N84 to A273. A structure analysis reveals that the "core domain" shares a high degree of structural similarity with chlamydial deubiquitinating enzyme, sentrin-specific protease, and adenovirus protease, while the "arm domain" is unique to ASFV. Further, experiments indicated that the "arm domain" plays an important role in maintaining the enzyme activity of ASFV pS273R. Moreover, based on the structural information of pS273R, we designed and synthesized several peptidomimetic aldehyde compounds at a submolar IC50 value, which paves the way for the design of inhibitors to target this severe pathogen.IMPORTANCEAfrican swine fever virus, a large and complex icosahedral DNA virus, causes a deadly infection in domestic pigs. In addition to Africa and Europe, countries in Asia, including China, Vietnam, and Mongolia, were negatively affected by the hazards posed by ASFV outbreaks in 2018-2019, at which time more than 30 million pigs were culled. Until now, there has been no vaccine for protection against ASFV infection or effective treatments to cure ASF. Here, we solved the high-resolution crystal structure of the ASFV pS273R protease. The pS273R protease has a two-domain structure that distinguishes it from other members of the SUMO protease family, while the unique "arm domain" has been proven to be essential for its hydrolytic activity. Moreover, the peptidomimetic aldehyde compounds designed to target the substrate binding pocket exert prominent inhibitory effects and can thus be used in a potential lead for anti-ASFV drug development.

Crystal structure of the African swine fever virus pS273R protease and implications for inhibitor design.,Li G, Liu X, Yang M, Zhang G, Wang Z, Guo K, Gao Y, Jiao P, Sun J, Chen C, Wang H, Deng W, Xiao H, Li S, Wu H, Wang Y, Cao L, Jia Z, Shang L, Yang C, Guo Y, Rao Z J Virol. 2020 Feb 19. pii: JVI.02125-19. doi: 10.1128/JVI.02125-19. PMID:32075933<ref>PMID:32075933</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 6ljb" style="background-color:#fffaf0;"></div>

==See Also==
*[[Virus proteases 3D strutures|Virus proteases 3D strutures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Asfk5]]
[[Category: Large Structures]]
[[Category: Chen, C]]
[[Category: Guo, Y]]
[[Category: Li, G B]]
[[Category: Liu, X X]]
[[Category: Asfv]]
[[Category: Hydrolase]]
[[Category: Ps273r protease]]