1gqp
From Proteopedia
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| - | [[Image:1gqp.gif|left|200px]] | + | [[Image:1gqp.gif|left|200px]] |
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| - | '''APC10/DOC1 SUBUNIT OF S. CEREVISIAE''' | + | {{Structure |
| + | |PDB= 1gqp |SIZE=350|CAPTION= <scene name='initialview01'>1gqp</scene>, resolution 2.20Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=BR:BROMIDE ION'>BR</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''APC10/DOC1 SUBUNIT OF S. CEREVISIAE''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1GQP is a [ | + | 1GQP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GQP OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11884135 11884135] |
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: ubiquitination]] | [[Category: ubiquitination]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:26:43 2008'' |
Revision as of 09:26, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
APC10/DOC1 SUBUNIT OF S. CEREVISIAE
Overview
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.
About this Structure
1GQP is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
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
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