2g62: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
(2 intermediate revisions by the same user not shown)
Line 1: Line 1:
==Crystal structure of human PTPA==
==Crystal structure of human PTPA==
<StructureSection load='2g62' size='340' side='right' caption='[[2g62]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
<StructureSection load='2g62' size='340' side='right'caption='[[2g62]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2g62]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2G62 FirstGlance]. <br>
<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>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</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>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PPP2R4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<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>
<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=2g62 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g62 OCA], [http://pdbe.org/2g62 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2g62 RCSB], [http://www.ebi.ac.uk/pdbsum/2g62 PDBsum]</span></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=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>
</table>
== Function ==
== Function ==
[[http://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>
[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g6/2g62_consurf.spt"</scriptWhenChecked>
     <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>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
Line 19: Line 20:
</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].
</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>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Protein phosphatase 2A (PP2A) is a heterotrimeric Ser/Thr phosphatase that is involved in regulating a plethora of signaling pathways in the cell, making its regulation a critical part of the well being of the cell. For example, three of the non-catalytic PP2A subunits have been linked to carcinogenic events. Therefore, the molecular basis for the complicated protein-protein interaction pattern of PP2A and its regulators is of special interest. The PP2A phosphatase activator (PTPA) protein is highly conserved from humans to yeast. It is an activator of PP2A and has been shown to be essential for a fully functional PP2A, but its mechanism of activation is still not well defined. We have solved the crystal structure of human PTPA to 1.6A. It reveals a two-domain protein with a novel fold comprised of 13 alpha-helices. We have identified a highly conserved cleft as a potential region for interaction with peptide segments of other proteins. Binding studies with ATP and its analogs are not consistent with ATP being a cofactor/substrate for PTPA as had previously been proposed. The structure of PTPA can serve as a basis for structure-function studies directed at elucidating its mechanism as an activator of PP2A.
The crystal structure of a human PP2A phosphatase activator reveals a novel fold and highly conserved cleft implicated in protein-protein interactions.,Magnusdottir A, Stenmark P, Flodin S, Nyman T, Hammarstrom M, Ehn M, Bakali H MA, Berglund H, Nordlund P J Biol Chem. 2006 Aug 11;281(32):22434-8. Epub 2006 Jun 16. PMID:16782712<ref>PMID:16782712</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2g62" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Protein phosphatase|Protein phosphatase]]
*[[Protein phosphatase 3D structures|Protein phosphatase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[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]]

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

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=2g62&oldid=4088940"