1c25
From Proteopedia
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|SITE= <scene name='pdbsite=DSU:CYS+A+384+And+CYS+A+340+May+Form+Disulfide+Bond+Under+Ce+...'>DSU</scene> and <scene name='pdbsite=POP:Putative+Phosphate+Binding+Loop,+CYS-X(5)-ARG+Signature+...'>POP</scene> | |SITE= <scene name='pdbsite=DSU:CYS+A+384+And+CYS+A+340+May+Form+Disulfide+Bond+Under+Ce+...'>DSU</scene> and <scene name='pdbsite=POP:Putative+Phosphate+Binding+Loop,+CYS-X(5)-ARG+Signature+...'>POP</scene> | ||
|LIGAND= | |LIGAND= | ||
- | |ACTIVITY= [http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] </span> |
|GENE= CDC25A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= CDC25A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY= | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1c25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c25 OCA], [http://www.ebi.ac.uk/pdbsum/1c25 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1c25 RCSB]</span> | ||
}} | }} | ||
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[[Category: Saper, M A.]] | [[Category: Saper, M A.]] | ||
[[Category: cdk2]] | [[Category: cdk2]] | ||
- | [[Category: cell cycle phosphatase | + | [[Category: cell cycle phosphatase,dual specificity protein phosphatase]] |
- | + | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:13:01 2008'' |
Revision as of 16:13, 30 March 2008
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, resolution 2.3Å | |||||||
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Sites: | and | ||||||
Gene: | CDC25A (Homo sapiens) | ||||||
Activity: | Protein-tyrosine-phosphatase, with EC number 3.1.3.48 | ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
HUMAN CDC25A CATALYTIC DOMAIN
Overview
Cdc25 phosphatases activate the cell division kinases throughout the cell cycle. The 2.3 A structure of the human Cdc25A catalytic domain reveals a small alpha/beta domain with a fold unlike previously described phosphatase structures but identical to rhodanese, a sulfur-transfer protein. Only the active-site loop, containing the Cys-(X)5-Arg motif, shows similarity to the tyrosine phosphatases. In some crystals, the catalytic Cys-430 forms a disulfide bond with the invariant Cys-384, suggesting that Cdc25 may be self-inhibited during oxidative stress. Asp-383, previously proposed to be the general acid, instead serves a structural role, forming a conserved buried salt-bridge. We propose that Glu-431 may act as a general acid. Structure-based alignments suggest that the noncatalytic domain of the MAP kinase phosphatases will share this topology, as will ACR2, a eukaryotic arsenical resistance protein.
About this Structure
1C25 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the catalytic domain of the human cell cycle control phosphatase, Cdc25A., Fauman EB, Cogswell JP, Lovejoy B, Rocque WJ, Holmes W, Montana VG, Piwnica-Worms H, Rink MJ, Saper MA, Cell. 1998 May 15;93(4):617-25. PMID:9604936
Page seeded by OCA on Sun Mar 30 19:13:01 2008