1ohd

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[[Category: protein phosphatase]]
[[Category: protein phosphatase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:08:34 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:54:28 2007''

Revision as of 13:49, 30 October 2007


1ohd, resolution 2.60Å

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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 ... [(full description)]

About this Structure

1OHD is a [Single protein] structure of sequence from [Homo sapiens] with WO4 as [ligand]. Structure known Active Site: AC1. 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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