2g62: Difference between revisions

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[[Image:2g62.png|left|200px]]


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==Crystal structure of human PTPA==
The line below this paragraph, containing "STRUCTURE_2g62", creates the "Structure Box" on the page.
<StructureSection load='2g62' size='340' side='right'caption='[[2g62]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2g62]] 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=2G62 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2G62 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
{{STRUCTURE_2g62| PDB=2g62 |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2g62 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g62 OCA], [https://pdbe.org/2g62 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2g62 RCSB], [https://www.ebi.ac.uk/pdbsum/2g62 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2g62 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PTPA_HUMAN PTPA_HUMAN] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for serine/threonine-protein phosphatase 2A (PP2A) modulating its activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a proposed direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2A(i)) in presence of ATP and Mg(2+) (By similarity). Reversibly stimulates the variable phosphotyrosyl phosphatase activity of PP2A core heterodimer PP2A(D) in presence of ATP and Mg(2+) (in vitro). The phosphotyrosyl phosphatase activity is dependent of an ATPase activity of the PP2A(D):PPP2R4 complex. Is involved in apoptosis; the function appears to be independent from PP2A.<ref>PMID:17333320</ref> <ref>PMID:16916641</ref>
== 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/g6/2g62_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=2g62 ConSurf].
<div style="clear:both"></div>


===Crystal structure of human PTPA===
==See Also==
 
*[[Protein phosphatase 3D structures|Protein phosphatase 3D structures]]
 
== References ==
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{{ABSTRACT_PUBMED_16782712}}
 
==About this Structure==
2G62 is a 1 chain 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=2G62 OCA].
 
==Reference==
<ref group="xtra">PMID:16782712</ref><references group="xtra"/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Arrowsmith, C.]]
[[Category: Large Structures]]
[[Category: Berg, S Van Den.]]
[[Category: Arrowsmith C]]
[[Category: Berglund, H.]]
[[Category: Berglund H]]
[[Category: Collins, R.]]
[[Category: Collins R]]
[[Category: Edwards, A.]]
[[Category: Edwards A]]
[[Category: Ehn, M.]]
[[Category: Ehn M]]
[[Category: Flodin, S.]]
[[Category: Flodin S]]
[[Category: Flores, A.]]
[[Category: Flores A]]
[[Category: G Thorsell, A.]]
[[Category: Graslund S]]
[[Category: Graslund, S.]]
[[Category: Hallberg BM]]
[[Category: Hallberg, B M.]]
[[Category: Hammarstrom M]]
[[Category: Hammarstrom, M.]]
[[Category: Hogbom M]]
[[Category: Hogbom, M.]]
[[Category: Holmberg Schiavone L]]
[[Category: Kotenyova, T.]]
[[Category: Kotenyova T]]
[[Category: Magnusdottir, A.]]
[[Category: Magnusdottir A]]
[[Category: Nilsson-Ehle, P.]]
[[Category: Nilsson-Ehle P]]
[[Category: Nordlund, P.]]
[[Category: Nordlund P]]
[[Category: Nyman, T.]]
[[Category: Nyman T]]
[[Category: Ogg, D.]]
[[Category: Ogg D]]
[[Category: Persson, C.]]
[[Category: Persson C]]
[[Category: Sagemark, J.]]
[[Category: Sagemark J]]
[[Category: Schiavone, L Holmberg.]]
[[Category: Stenmark P]]
[[Category: Stenmark, P.]]
[[Category: Sundstrom M]]
[[Category: Sundstrom, M.]]
[[Category: Thorsell AG]]
[[Category: Wallden, K.]]
[[Category: Van Den Berg S]]
[[Category: Weigelt, J.]]
[[Category: Wallden K]]
[[Category: Hydrolase activator]]
[[Category: Weigelt J]]
[[Category: Mgc2184]]
[[Category: Pp2a]]
[[Category: Ppp2r4]]
[[Category: Pr53]]
[[Category: Protein phosphatase 2a]]
[[Category: Ptpa]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 21:09:05 2009''

Latest revision as of 16:51, 13 March 2024

Crystal structure of human PTPACrystal structure of human PTPA

Structural highlights

2g62 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 1.6Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PTPA_HUMAN PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for serine/threonine-protein phosphatase 2A (PP2A) modulating its activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a proposed direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2A(i)) in presence of ATP and Mg(2+) (By similarity). Reversibly stimulates the variable phosphotyrosyl phosphatase activity of PP2A core heterodimer PP2A(D) in presence of ATP and Mg(2+) (in vitro). The phosphotyrosyl phosphatase activity is dependent of an ATPase activity of the PP2A(D):PPP2R4 complex. Is involved in apoptosis; the function appears to be independent from PP2A.[1] [2]

Evolutionary Conservation

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

See Also

References

  1. ↑ Azam S, Drobetsky E, Ramotar D. Overexpression of the cis/trans isomerase PTPA triggers caspase 3-dependent apoptosis. Apoptosis. 2007 Jul;12(7):1243-55. PMID:17333320 doi:http://dx.doi.org/10.1007/s10495-006-0050-8
  2. ↑ Chao Y, Xing Y, Chen Y, Xu Y, Lin Z, Li Z, Jeffrey PD, Stock JB, Shi Y. Structure and mechanism of the phosphotyrosyl phosphatase activator. Mol Cell. 2006 Aug;23(4):535-46. PMID:16916641 doi:http://dx.doi.org/10.1016/j.molcel.2006.07.027

2g62, resolution 1.60Å

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