1c25: Difference between revisions

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[[Image:1c25.gif|left|200px]]


{{Structure
==HUMAN CDC25A CATALYTIC DOMAIN==
|PDB= 1c25 |SIZE=350|CAPTION= <scene name='initialview01'>1c25</scene>, resolution 2.3&Aring;
<StructureSection load='1c25' size='340' side='right'caption='[[1c25]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
|SITE= <scene name='pdbsite=DSU:CYS+A+384+And+CYS+A+340+May+Form+Disulfide+Bond+Under+Ce+...'>DSU</scene> and <scene name='pdbsite=POP:Putative+Phosphate+Binding+Loop,+CYS-X(5)-ARG+Signature+...'>POP</scene>
== Structural highlights ==
|LIGAND=
<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>
|ACTIVITY= <span class='plainlinks'>[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] </span>
</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>
|GENE= CDC25A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
<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>
|DOMAIN=
</table>
|RELATEDENTRY=
== Function ==
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1c25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c25 OCA], [http://www.ebi.ac.uk/pdbsum/1c25 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1c25 RCSB]</span>
[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>


'''HUMAN CDC25A CATALYTIC DOMAIN'''
==See Also==
 
*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
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 noncatalytic domain of the MAP kinase phosphatases will share this topology, as will ACR2, a eukaryotic arsenical resistance protein.
 
==About this Structure==
1C25 is a [[Single protein]] structure of sequence from [http://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].
 
==Reference==
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://www.ncbi.nlm.nih.gov/pubmed/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,dual specificity protein phosphatase]]
[[Category: hydrolase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:13:01 2008''

Latest revision as of 06:40, 7 February 2024

HUMAN CDC25A CATALYTIC DOMAIN

1c25, resolution 2.30Å

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