2qiy: Difference between revisions
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<StructureSection load='2qiy' size='340' side='right'caption='[[2qiy]], [[Resolution|resolution]] 1.69Å' scene=''> | <StructureSection load='2qiy' size='340' side='right'caption='[[2qiy]], [[Resolution|resolution]] 1.69Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2qiy]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2qiy]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QIY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QIY FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.69Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2qiy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qiy OCA], [https://pdbe.org/2qiy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qiy RCSB], [https://www.ebi.ac.uk/pdbsum/2qiy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qiy ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2qiy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qiy OCA], [https://pdbe.org/2qiy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qiy RCSB], [https://www.ebi.ac.uk/pdbsum/2qiy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qiy ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/BRE5_YEAST BRE5_YEAST] Has a role in de-ubiquitination. In conjunction with UBP3, cleaves ubiquitin, leading to the subsequent mono-ubiquitination of sec23.<ref>PMID:12778054</ref> | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Li | [[Category: Li K]] | ||
[[Category: Liu | [[Category: Liu X]] | ||
[[Category: Marmorstein | [[Category: Marmorstein R]] | ||
Latest revision as of 14:33, 30 August 2023
yeast Deubiquitinase Ubp3 and Bre5 cofactor complexyeast Deubiquitinase Ubp3 and Bre5 cofactor complex
Structural highlights
FunctionBRE5_YEAST Has a role in de-ubiquitination. In conjunction with UBP3, cleaves ubiquitin, leading to the subsequent mono-ubiquitination of sec23.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedYeast Ubp3 and its co-factor Bre5 form a deubiquitylation complex to regulate protein transport between the endoplasmic reticulum and Golgi compartments of the cell. A novel N-terminal domain of the Ubp3 catalytic subunit forms a complex with the NTF2-like domain of the Bre5 regulatory subunit. Here, we report the X-ray crystal structure of an Ubp3-Bre5 complex and show that it forms a symmetric hetero-tetrameric complex in which the Bre5 NTF2-like domain dimer interacts with two L-shaped beta-strand-turn-alpha-helix motifs of Ubp3. The Ubp3 N-terminal domain binds within a hydrophobic cavity on the surface of the Bre5 NTF2-like domain subunit with conserved residues within both proteins interacting predominantly through antiparallel beta-sheet hydrogen bonds and van der Waals contacts. Structure-based mutagenesis and functional studies confirm the significance of the observed interactions for Ubp3-Bre5 association in vitro and Ubp3 function in vivo. Comparison of the structure to other protein complexes with NTF2-like domains shows that the Ubp3-Bre5 interface is novel. Together, these studies provide new insights into Ubp3 recognition by Bre5 and into protein recognition by NTF2-like domains. Molecular basis for bre5 cofactor recognition by the ubp3 deubiquitylating enzyme.,Li K, Ossareh-Nazari B, Liu X, Dargemont C, Marmorstein R J Mol Biol. 2007 Sep 7;372(1):194-204. Epub 2007 Jun 27. PMID:17632125[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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