1ohd

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[[Image:1ohd.jpg|left|200px]]
[[Image:1ohd.jpg|left|200px]]
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{{Structure
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|PDB= 1ohd |SIZE=350|CAPTION= <scene name='initialview01'>1ohd</scene>, resolution 2.60&Aring;
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The line below this paragraph, containing "STRUCTURE_1ohd", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:Wo4+Binding+Site+For+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=WO4:TUNGSTATE(VI)ION'>WO4</scene>
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{{STRUCTURE_1ohd| PDB=1ohd | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ohd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ohd OCA], [http://www.ebi.ac.uk/pdbsum/1ohd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ohd RCSB]</span>
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'''STRUCTURE OF CDC14 IN COMPLEX WITH TUNGSTATE'''
'''STRUCTURE OF CDC14 IN COMPLEX WITH TUNGSTATE'''
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[[Category: Gray, C.]]
[[Category: Gray, C.]]
[[Category: Tonks, N.]]
[[Category: Tonks, N.]]
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[[Category: cell cycle]]
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[[Category: Cell cycle]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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[[Category: protein phosphatase]]
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[[Category: Protein phosphatase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:50:56 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:45:22 2008''
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Revision as of 00:50, 3 May 2008

Image:1ohd.jpg

Template:STRUCTURE 1ohd

STRUCTURE OF CDC14 IN COMPLEX WITH TUNGSTATE


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

1OHD 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 Page seeded by OCA on Sat May 3 03:50:56 2008

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