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1ohe

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Revision as of 07:09, 7 February 2018

Structure of cdc14b phosphatase with a peptide ligand

Structural highlights

1ohe is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:	,
Related:	1ohc, 1ohd
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CC14B_HUMAN] Dual-specificity phosphatase involved in DNA damage response. Essential regulator of the G2 DNA damage checkpoint: following DNA damage, translocates to the nucleus and dephosphorylates FZR1/CDH1, a key activator of the anaphase promoting complex/cyclosome (APC/C). Dephosphorylation of FZR1/CDH1 activates the APC/C, leading to the ubiquitination of PLK1, preventing entry into mitosis. Preferentially dephosphorylates proteins modified by proline-directed kinases.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Li L, Ernsting BR, Wishart MJ, Lohse DL, Dixon JE. A family of putative tumor suppressors is structurally and functionally conserved in humans and yeast. J Biol Chem. 1997 Nov 21;272(47):29403-6. PMID:9367992
↑ Bassermann F, Frescas D, Guardavaccaro D, Busino L, Peschiaroli A, Pagano M. The Cdc14B-Cdh1-Plk1 axis controls the G2 DNA-damage-response checkpoint. Cell. 2008 Jul 25;134(2):256-67. doi: 10.1016/j.cell.2008.05.043. PMID:18662541 doi:http://dx.doi.org/10.1016/j.cell.2008.05.043
↑ Gray CH, Good VM, Tonks NK, Barford D. The structure of the cell cycle protein Cdc14 reveals a proline-directed protein phosphatase. EMBO J. 2003 Jul 15;22(14):3524-35. PMID:12853468 doi:10.1093/emboj/cdg348

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ohe"

@@ Line 1: / Line 1: @@
-==STRUCTURE OF CDC14B PHOSPHATASE WITH A PEPTIDE LIGAND==
+==Structure of cdc14b phosphatase with a peptide ligand==
 <StructureSection load='1ohe' size='340' side='right' caption='[[1ohe]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
@@ Line 5: / Line 6: @@
 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ohc|1ohc]], [[1ohd|1ohd]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ohe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ohe OCA], [http://pdbe.org/1ohe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ohe RCSB], [http://www.ebi.ac.uk/pdbsum/1ohe PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ohe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ohe OCA], [http://pdbe.org/1ohe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ohe RCSB], [http://www.ebi.ac.uk/pdbsum/1ohe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ohe ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 13: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oh/1ohe_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oh/1ohe_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 28: / Line 29: @@
 </div>
 <div class="pdbe-citations 1ohe" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Dual specificity phosphatase|Dual specificity phosphatase]]
 == References ==
 <references/>

1ohe

From Proteopedia

Revision as of 07:09, 7 February 2018

Structure of cdc14b phosphatase with a peptide ligand

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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