1ohc
From Proteopedia
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| - | [[Image:1ohc.jpg|left|200px]] | + | [[Image:1ohc.jpg|left|200px]] |
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| - | '''STRUCTURE OF THE PROLINE DIRECTED PHOSPHATASE CDC14''' | + | {{Structure |
| + | |PDB= 1ohc |SIZE=350|CAPTION= <scene name='initialview01'>1ohc</scene>, resolution 2.50Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''STRUCTURE OF THE PROLINE DIRECTED PHOSPHATASE CDC14''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1OHC is a [ | + | 1OHC 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=1OHC OCA]. |
==Reference== | ==Reference== | ||
| - | The structure of the cell cycle protein Cdc14 reveals a proline-directed protein phosphatase., Gray CH, Good VM, Tonks NK, Barford D, EMBO J. 2003 Jul 15;22(14):3524-35. PMID:[http:// | + | The structure of the cell cycle protein Cdc14 reveals a proline-directed protein phosphatase., Gray CH, Good VM, Tonks NK, Barford D, EMBO J. 2003 Jul 15;22(14):3524-35. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12853468 12853468] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''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 13:10:53 2008'' |
Revision as of 11:10, 20 March 2008
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| , resolution 2.50Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF THE PROLINE DIRECTED PHOSPHATASE CDC14
Overview
The Cdc14 family of dual-specificity protein phosphatases (DSPs) is conserved within eukaryotes and functions to down-regulate mitotic Cdk activities, promoting cytokinesis and mitotic exit. We have integrated structural and kinetic analyses to define the molecular mechanism of the dephosphorylation reaction catalysed by Cdc14. The structure of Cdc14 illustrates a novel arrangement of two domains, each with a DSP-like fold, arranged in tandem. The C-terminal domain contains the conserved PTP motif of the catalytic site, whereas the N-terminal domain, which shares no sequence similarity with other DSPs, contributes to substrate specificity, and lacks catalytic activity. The catalytic site is located at the base of a pronounced surface channel formed by the interface of the two domains, and regions of both domains interact with the phosphopeptide substrate. Specificity for a pSer-Pro motif is mediated by a hydrophobic pocket that is capable of accommodating the apolar Pro(P+1) residue of the peptide. Our structural and kinetic data support a role for Cdc14 in the preferential dephosphorylation of proteins modified by proline-directed kinases.
About this Structure
1OHC is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The structure of the cell cycle protein Cdc14 reveals a proline-directed protein phosphatase., Gray CH, Good VM, Tonks NK, Barford D, EMBO J. 2003 Jul 15;22(14):3524-35. PMID:12853468
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