1c25: Difference between revisions

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[[Image:1c25.gif|left|200px]]<br />
<applet load="1c25" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1c25, resolution 2.3&Aring;" />
'''HUMAN CDC25A CATALYTIC DOMAIN'''<br />


==Overview==
==HUMAN CDC25A CATALYTIC DOMAIN==
Cdc25 phosphatases activate the cell division kinases throughout the cell, cycle. The 2.3 A structure of the human Cdc25A catalytic domain reveals a, small alpha/beta domain with a fold unlike previously described, phosphatase structures but identical to rhodanese, a sulfur-transfer, protein. Only the active-site loop, containing the Cys-(X)5-Arg motif, shows similarity to the tyrosine phosphatases. In some crystals, the, catalytic Cys-430 forms a disulfide bond with the invariant Cys-384, suggesting that Cdc25 may be self-inhibited during oxidative stress., Asp-383, previously proposed to be the general acid, instead serves a, structural role, forming a conserved buried salt-bridge. We propose that, Glu-431 may act as a general acid. Structure-based alignments suggest that, the ... [[http://ispc.weizmann.ac.il/pmbin/getpm?9604936 (full description)]]
<StructureSection load='1c25' size='340' side='right'caption='[[1c25]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1c25]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C25 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C25 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1c25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c25 OCA], [https://pdbe.org/1c25 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c25 RCSB], [https://www.ebi.ac.uk/pdbsum/1c25 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c25 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MPIP1_HUMAN MPIP1_HUMAN] Tyrosine protein phosphatase which functions as a dosage-dependent inducer of mitotic progression. Directly dephosphorylates CDK1 and stimulates its kinase activity. Also dephosphorylates CDK2 in complex with cyclin E, in vitro.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c2/1c25_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1c25 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1C25 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]]. Active as [[http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48]]. Structure known Active Sites: DSU and POP. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1C25 OCA]].
*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Crystal structure of the catalytic domain of the human cell cycle control phosphatase, Cdc25A., Fauman EB, Cogswell JP, Lovejoy B, Rocque WJ, Holmes W, Montana VG, Piwnica-Worms H, Rink MJ, Saper MA, Cell. 1998 May 15;93(4):617-25. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9604936 9604936]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein-tyrosine-phosphatase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Cogswell JP]]
[[Category: Cogswell, J.P.]]
[[Category: Fauman EB]]
[[Category: Fauman, E.B.]]
[[Category: Holmes W]]
[[Category: Holmes, W.]]
[[Category: Lovejoy B]]
[[Category: Lovejoy, B.]]
[[Category: Montana VG]]
[[Category: Montana, V.G.]]
[[Category: Piwnica-Worms H]]
[[Category: Piwnica-Worms, H.]]
[[Category: Rink MJ]]
[[Category: Rink, M.J.]]
[[Category: Rocque WJ]]
[[Category: Rocque, W.J.]]
[[Category: Saper MA]]
[[Category: Saper, M.A.]]
[[Category: cdk2]]
[[Category: cell cycle phosphatase]]
[[Category: dual specificity protein phosphatase]]
[[Category: hydrolase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:48:03 2007''

Latest revision as of 09:40, 7 February 2024

HUMAN CDC25A CATALYTIC DOMAINHUMAN CDC25A CATALYTIC DOMAIN

Structural highlights

1c25 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MPIP1_HUMAN Tyrosine protein phosphatase which functions as a dosage-dependent inducer of mitotic progression. Directly dephosphorylates CDK1 and stimulates its kinase activity. Also dephosphorylates CDK2 in complex with cyclin E, in vitro.

Evolutionary Conservation

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

See Also

1c25, resolution 2.30Å

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