1jhj: Difference between revisions
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==Crystal structure of the APC10/Doc1 subunit of the human anaphase-promoting complex== | ==Crystal structure of the APC10/Doc1 subunit of the human anaphase-promoting complex== | ||
<StructureSection load='1jhj' size='340' side='right' caption='[[1jhj]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='1jhj' size='340' side='right' caption='[[1jhj]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1jhj]] is a 1 chain structure | <table><tr><td colspan='2'>[[1jhj]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JHJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JHJ FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></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=1jhj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jhj OCA], [http://pdbe.org/1jhj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jhj RCSB], [http://www.ebi.ac.uk/pdbsum/1jhj 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=1jhj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jhj OCA], [http://pdbe.org/1jhj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jhj RCSB], [http://www.ebi.ac.uk/pdbsum/1jhj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jhj ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Gieffers, C]] | [[Category: Gieffers, C]] | ||
[[Category: Gmachl, M]] | [[Category: Gmachl, M]] | ||
Revision as of 10:14, 29 March 2017
Crystal structure of the APC10/Doc1 subunit of the human anaphase-promoting complexCrystal structure of the APC10/Doc1 subunit of the human anaphase-promoting complex
Structural highlights
Function[APC10_HUMAN] Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains.[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 PubMedThe anaphase-promoting complex (APC), or cyclosome, is a cell cycle-regulated ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC is composed of at least 11 subunits; no structure has been determined for any of these subunits. The subunit APC10/DOC1, a one-domain protein consisting of 185 amino acids, has a conserved core (residues 22-161) that is homologous to domains found in several other putative ubiquitin ligases and, therefore, may play a role in ubiquitination reactions. Here we report the crystal structure of human APC10 at 1.6 A resolution. The core of the protein is formed by a beta-sandwich that adopts a jellyroll fold. Unexpectedly, this structure is highly similar to ligand-binding domains of several bacterial and eukaryotic proteins, such as galactose oxidase and coagulation factor Va, raising the possibility that APC10 may function by binding a yet unidentified ligand. We further provide biochemical evidence that the C-terminus of APC10 binds to CDC27/APC3, an APC subunit that contains multiple tetratrico peptide repeats. Crystal structure of the APC10/DOC1 subunit of the human anaphase-promoting complex.,Wendt KS, Vodermaier HC, Jacob U, Gieffers C, Gmachl M, Peters JM, Huber R, Sondermann P Nat Struct Biol. 2001 Sep;8(9):784-8. PMID:11524682[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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