5lwa
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==TURNIP YELLOW MOSAIC VIRUS PROTEASE/DEUBIQUITINASE DOMAIN, I847A MUTANT== | |
| + | <StructureSection load='5lwa' size='340' side='right' caption='[[5lwa]], [[Resolution|resolution]] 1.65Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5lwa]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LWA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LWA FirstGlance]. <br> | ||
| + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4a5u|4a5u]], [[5lw5|5lw5]]</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=5lwa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lwa OCA], [http://pdbe.org/5lwa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lwa RCSB], [http://www.ebi.ac.uk/pdbsum/5lwa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lwa ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/POLR_TYMV POLR_TYMV]] Acts as a cysteine protease, methyltransferase and deubiquitinase. The cyteine protease activity cleaves the polyprotein giving rise to mature proteins. The methyltransferase domain is probably involved in viral RNA capping. The deubiquitylating activity counteracts the degradation of the viral polymerase mediated by the host ubiquitin-proteasome system. The polymerase is thus stabilized and infectivity is increased.<ref>PMID:22117220</ref> RNA-directed RNA polymerase is responsible for the replication and transcription of the genome.<ref>PMID:22117220</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Processing of the polyprotein of Turnip yellow mosaic virus is mediated by the protease PRO. PRO cleaves at two places, one of which is at the C-terminus of the PRO domain of another polyprotein molecule. In addition to this processing activity, PRO possesses an ubiquitin hydrolase (DUB) activity. The crystal structure of PRO has previously been reported in its polyprotein-processing mode with the C-terminus of one PRO inserted into the catalytic site of the next PRO, generating PRO polymers in the crystal packing of the trigonal space group. Here, two mutants designed to disrupt specific PRO-PRO interactions were generated, produced and purified. Crystalline plates were obtained by seeding and cross-seeding from initial `sea urchin'-like microcrystals of one mutant. The plates diffracted to beyond 2 A resolution at a synchrotron source and complete data sets were collected for the two mutants. Data processing and analysis indicated that both mutant crystals belonged to the same monoclinic space group, with two molecules of PRO in the asymmetric unit. | ||
| - | + | Crystallization of mutants of Turnip yellow mosaic virus protease/ubiquitin hydrolase designed to prevent protease self-recognition.,Ayach M, Bressanelli S Acta Crystallogr F Struct Biol Commun. 2015 Apr;71(Pt 4):405-8. doi:, 10.1107/S2053230X15003945. Epub 2015 Mar 20. PMID:25849500<ref>PMID:25849500</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5lwa" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Ayach, M]] | [[Category: Ayach, M]] | ||
| + | [[Category: Bressanelli, S]] | ||
| + | [[Category: Cysteine protease]] | ||
| + | [[Category: Deubiquitinase]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Virus replicase polyprotein]] | ||
Revision as of 07:11, 25 October 2017
TURNIP YELLOW MOSAIC VIRUS PROTEASE/DEUBIQUITINASE DOMAIN, I847A MUTANT
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