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1jhj
From Proteopedia
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| - | [[Image:1jhj.jpg|left|200px]] | + | [[Image:1jhj.jpg|left|200px]] |
| - | + | ||
| - | '''Crystal structure of the APC10/Doc1 subunit of the human anaphase-promoting complex''' | + | {{Structure |
| + | |PDB= 1jhj |SIZE=350|CAPTION= <scene name='initialview01'>1jhj</scene>, resolution 1.6Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=NI:NICKEL (II) ION'>NI</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of the APC10/Doc1 subunit of the human anaphase-promoting complex''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1JHJ is a [ | + | 1JHJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JHJ OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11524682 11524682] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: jellyroll]] | [[Category: jellyroll]] | ||
| - | ''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 12:03:29 2008'' |
Revision as of 10:03, 20 March 2008
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| , resolution 1.6Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the APC10/Doc1 subunit of the human anaphase-promoting complex
Overview
The 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.
About this Structure
1JHJ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
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