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1gqp

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Revision as of 06:59, 16 November 2017

APC10/DOC1 SUBUNIT OF S. cerevisiae

Structural highlights

1gqp is a 2 chain structure with sequence from Atcc 18824. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[APC10_YEAST] Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. In early mitosis, the APC/C is activated by CDC20 and targets securin PDS1, the B-type cyclin CLB5, and other anaphase inhibitory proteins for proteolysis, thereby triggering the separation of sister chromatids at the metaphase-to-anaphase transition. In late mitosis and in G1, degradation of CLB5 allows activation of the APC/C by CDH1, which is needed to destroy CDC20 and the B-type cyclin CLB2 to allow exit from mitosis and creating the low CDK state necessary for cytokinesis and for reforming prereplicative complexes in G1 prior to another round of replication. DOC1 is required, together with the coactivators CDH1 and CDC20, for recognition and binding of the substrates.^[1] ^[2]

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 PubMed

The anaphase-promoting complex (APC) is a multi-subunit E3 protein ubiquitin ligase that is responsible for the metaphase to anaphase transition and the exit from mitosis. One of the subunits of the APC that is required for its ubiquitination activity is Doc1/Apc10, a protein composed of a Doc1 homology domain that has been identified in a number of diverse putative E3 ubiquitin ligases. Here, we present the crystal structure of Saccharomyces cerevisiae Doc1/Apc10 at 2.2A resolution. The Doc1 homology domain forms a beta-sandwich structure that is related in architecture to the galactose-binding domain of galactose oxidase, the coagulation factor C2 domain and a domain of XRCC1. Residues that are invariant amongst Doc1/Apc10 sequences, including a temperature-sensitive mitotic arrest mutant, map to a beta-sheet region of the molecule, whose counterpart in galactose oxidase, the coagulation factor C2 domains and XRCC1, mediate bio-molecular interactions. This finding suggests the identification of the functionally important and conserved region of Doc1/Apc10 and, since invariant residues of Doc1/Apc10 colocalise with conserved residues of other Doc1 homology domains, we propose that the Doc1 homology domains perform common ubiquitination functions in the APC and other E3 ubiquitin ligases.

Implications for the ubiquitination reaction of the anaphase-promoting complex from the crystal structure of the Doc1/Apc10 subunit.,Au SW, Leng X, Harper JW, Barford D J Mol Biol. 2002 Mar 1;316(4):955-68. PMID:11884135^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Carroll CW, Morgan DO. The Doc1 subunit is a processivity factor for the anaphase-promoting complex. Nat Cell Biol. 2002 Nov;4(11):880-7. PMID:12402045 doi:http://dx.doi.org/10.1038/ncb871
↑ Passmore LA, McCormack EA, Au SW, Paul A, Willison KR, Harper JW, Barford D. Doc1 mediates the activity of the anaphase-promoting complex by contributing to substrate recognition. EMBO J. 2003 Feb 17;22(4):786-96. PMID:12574115 doi:http://dx.doi.org/10.1093/emboj/cdg084
↑ Au SW, Leng X, Harper JW, Barford D. Implications for the ubiquitination reaction of the anaphase-promoting complex from the crystal structure of the Doc1/Apc10 subunit. J Mol Biol. 2002 Mar 1;316(4):955-68. PMID:11884135 doi:10.1006/jmbi.2002.5399

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1gqp"

@@ Line 1: / Line 1: @@
-==APC10/DOC1 SUBUNIT OF S. CEREVISIAE==
+==APC10/DOC1 SUBUNIT OF S. cerevisiae==
 <StructureSection load='1gqp' size='340' side='right' caption='[[1gqp]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1gqp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GQP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GQP FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</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=1gqp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gqp OCA], [http://pdbe.org/1gqp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gqp RCSB], [http://www.ebi.ac.uk/pdbsum/1gqp 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=1gqp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gqp OCA], [http://pdbe.org/1gqp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gqp RCSB], [http://www.ebi.ac.uk/pdbsum/1gqp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1gqp ProSAT]</span></td></tr>
 </table>
 == Function ==

1gqp

From Proteopedia

Revision as of 06:59, 16 November 2017

APC10/DOC1 SUBUNIT OF S. cerevisiae

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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