3td7: Difference between revisions
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<StructureSection load='3td7' size='340' side='right' caption='[[3td7]], [[Resolution|resolution]] 2.21Å' scene=''> | <StructureSection load='3td7' size='340' side='right' caption='[[3td7]], [[Resolution|resolution]] 2.21Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3td7]] is a 1 chain structure | <table><tr><td colspan='2'>[[3td7]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TD7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TD7 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]], [[3p0k|3p0k]], [[3gwl|3gwl]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3gwn|3gwn]], [[3p0k|3p0k]], [[3gwl|3gwl]]</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=3td7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3td7 OCA], [http://pdbe.org/3td7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3td7 RCSB], [http://www.ebi.ac.uk/pdbsum/3td7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3td7 ProSAT]</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=3td7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3td7 OCA], [http://pdbe.org/3td7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3td7 RCSB], [http://www.ebi.ac.uk/pdbsum/3td7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3td7 ProSAT]</span></td></tr> | ||
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/YR596_MIMIV YR596_MIMIV]] FAD-dependent sulfhydryl oxidase that catalyzes disulfide bond formation (By similarity). | [[http://www.uniprot.org/uniprot/YR596_MIMIV YR596_MIMIV]] FAD-dependent sulfhydryl oxidase that catalyzes disulfide bond formation (By similarity). | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The mimivirus genome contains many genes that lack homologs in the sequence database and are thus known as ORFans. In addition, mimivirus genes that encode proteins belonging to known fold families are in some cases fused to domain-sized segments that cannot be classified. One such ORFan region is present in the mimivirus enzyme R596, a member of the Erv family of sulfhydryl oxidases. We determined the structure of a variant of full-length R596 and observed that the carboxy-terminal region of R596 assumes a folded, compact domain, demonstrating that these ORFan segments can be stable structural units. Moreover, the R596 ORFan domain fold is novel, hinting at the potential wealth of protein structural innovation yet to be discovered in large double-stranded DNA viruses. In the context of the R596 dimer, the ORFan domain contributes to formation of a broad cleft enriched with exposed aromatic groups and basic side chains, which may function in binding target proteins or localization of the enzyme within the virus factory or virions. Finally, we find evidence for an intermolecular dithiol/disulfide relay within the mimivirus R596 dimer, the first such extended, intersubunit redox-active site identified in a viral sulfhydryl oxidase. | |||
Exploring ORFan domains in giant viruses: structure of mimivirus sulfhydryl oxidase R596.,Hakim M, Ezerina D, Alon A, Vonshak O, Fass D PLoS One. 2012;7(11):e50649. doi: 10.1371/journal.pone.0050649. Epub 2012 Nov 28. PMID:23209798<ref>PMID:23209798</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3td7" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Sulfhydryl oxidase|Sulfhydryl oxidase]] | *[[Sulfhydryl oxidase|Sulfhydryl oxidase]] | ||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Thiol oxidase]] | [[Category: Thiol oxidase]] | ||
[[Category: Fass, D]] | [[Category: Fass, D]] | ||