5a4p: Difference between revisions
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<StructureSection load='5a4p' size='340' side='right'caption='[[5a4p]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='5a4p' size='340' side='right'caption='[[5a4p]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5a4p]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5a4p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A4P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A4P FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></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=5a4p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a4p OCA], [https://pdbe.org/5a4p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a4p RCSB], [https://www.ebi.ac.uk/pdbsum/5a4p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a4p ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/UBE2Z_HUMAN UBE2Z_HUMAN] Catalyzes the covalent attachment of ubiquitin to other proteins (By similarity). Specific substrate for UBA6, not charged with ubiquitin by UBE1. May be involved in apoptosis regulation.[PROSITE-ProRule:PRU00388]<ref>PMID:17464193</ref> <ref>PMID:17597759</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[ | *[[3D structures of ubiquitin conjugating enzyme|3D structures of ubiquitin conjugating enzyme]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Dewitte F]] | |||
[[Category: Dewitte | [[Category: Monte D]] | ||
[[Category: Monte | [[Category: Rucktooa P]] | ||
[[Category: Rucktooa | [[Category: Schelpe J]] | ||
[[Category: Schelpe | [[Category: Sixma TK]] | ||
[[Category: Sixma | |||
Revision as of 07:39, 25 May 2023
Structure of UBE2Z provides functional insight into specificity in the FAT10 conjugation machineryStructure of UBE2Z provides functional insight into specificity in the FAT10 conjugation machinery
Structural highlights
FunctionUBE2Z_HUMAN Catalyzes the covalent attachment of ubiquitin to other proteins (By similarity). Specific substrate for UBA6, not charged with ubiquitin by UBE1. May be involved in apoptosis regulation.[PROSITE-ProRule:PRU00388][1] [2] Publication Abstract from PubMedFAT10 conjugation, a post-translational modification analogous to ubiquitination, specifically requires UBA6 and UBE2Z as its activating (E1) and conjugating (E2) enzymes. Interestingly, these enzymes can also function in ubiquitination. We have determined the crystal structure of UBE2Z and report how the different domains of this E2 enzyme are organized. We further combine our structural data with mutational analyses to understand how specificity is achieved in the FAT10 conjugation pathway. We show that specificity towards UBA6 and UBE2Z lies within the C-terminal CYCI tetra-peptide in FAT10. We also demonstrate that this motif slows down transfer rates for FAT10 from UBA6 onto UBE2Z. Structure of UBE2Z provides functional insight into specificity in the FAT10 conjugation machinery.,Schelpe J, Monte D, Dewitte F, Sixma TK, Rucktooa P J Biol Chem. 2015 Nov 10. pii: jbc.M115.671545. PMID:26555268[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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