3gwl
From Proteopedia
(Difference between revisions)
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==Crystal structure of ASFV pB119L, a viral sulfhydryl oxidase== | ==Crystal structure of ASFV pB119L, a viral sulfhydryl oxidase== | ||
<StructureSection load='3gwl' size='340' side='right' caption='[[3gwl]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='3gwl' size='340' side='right' caption='[[3gwl]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3gwl]] is a 2 chain structure | + | <table><tr><td colspan='2'>[[3gwl]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GWL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3GWL FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3gwn|3gwn]], [[1jr8|1jr8]], [[1oqc|1oqc]], [[2hj3|2hj3]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3gwn|3gwn]], [[1jr8|1jr8]], [[1oqc|1oqc]], [[2hj3|2hj3]]</td></tr> | ||
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">9GL, B119L, Ba71V-073 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10498 ASFB7])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thiol_oxidase Thiol oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.3.2 1.8.3.2] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thiol_oxidase Thiol oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.3.2 1.8.3.2] </span></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=3gwl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gwl OCA], [http://pdbe.org/3gwl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3gwl RCSB], [http://www.ebi.ac.uk/pdbsum/3gwl PDBsum]</span></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=3gwl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gwl OCA], [http://pdbe.org/3gwl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3gwl RCSB], [http://www.ebi.ac.uk/pdbsum/3gwl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3gwl ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
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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=3gwl ConSurf]. | </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=3gwl ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Large double-stranded DNA viruses, including poxviruses and mimiviruses, encode enzymes to catalyze the formation of disulfide bonds in viral proteins produced in the cell cytosol, an atypical location for oxidative protein folding. These viral disulfide catalysts belong to a family of sulfhydryl oxidases that are dimers of a small five-helix fold containing a Cys-X-X-Cys motif juxtaposed to a flavin adenine dinucleotide cofactor. We report that the sulfhydryl oxidase pB119L from African swine fever virus (ASFV) uses for self-assembly surface different from that observed in homologs from mammals, plants, and fungi. Within a protein family, different packing interfaces for the same oligomerization state are extremely rare. We find that the alternate dimerization mode seen in ASFV pB119L is not characteristic of all viral sulfhydryl oxidases, as the flavin-binding domain from a mimivirus sulfhydryl oxidase assumes the same dimer structure as the known eukaryotic enzymes. ASFV pB119L demonstrates the potential of large double-stranded DNA viruses, which have faster mutation rates than their hosts and the tendency to incorporate host genes, to pioneer new protein folds and self-assembly modes. | ||
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| + | Dimer interface migration in a viral sulfhydryl oxidase.,Hakim M, Fass D J Mol Biol. 2009 Aug 28;391(4):758-68. Epub 2009 Jul 2. PMID:19576902<ref>PMID:19576902</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 3gwl" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Sulfhydryl oxidase|Sulfhydryl oxidase]] | *[[Sulfhydryl oxidase|Sulfhydryl oxidase]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Asfb7]] | ||
[[Category: Thiol oxidase]] | [[Category: Thiol oxidase]] | ||
[[Category: Fass, D]] | [[Category: Fass, D]] | ||
Revision as of 19:26, 9 December 2016
Crystal structure of ASFV pB119L, a viral sulfhydryl oxidase
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Categories: Thiol oxidase | Fass, D | Hakim, M | Disulfide bond | Fad | Five-helix bundle | Flavoprotein | Homodimer | Late protein | Oxidoreductase | Virulence
