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PDBsum entry 1ohc
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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The structure of the cell cycle protein cdc14 reveals a proline-Directed protein phosphatase.
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Authors
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C.H.Gray,
V.M.Good,
N.K.Tonks,
D.Barford.
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Ref.
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Embo J, 2003,
22,
3524-3535.
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PubMed id
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Abstract
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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.
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