2ixn: Difference between revisions

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<StructureSection load='2ixn' size='340' side='right'caption='[[2ixn]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
<StructureSection load='2ixn' size='340' side='right'caption='[[2ixn]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2ixn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IXN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IXN FirstGlance]. <br>
<table><tr><td colspan='2'>[[2ixn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IXN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IXN FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2ixo|2ixo]], [[2ixp|2ixp]]</div></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]] 2.8&#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=2ixn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ixn OCA], [https://pdbe.org/2ixn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ixn RCSB], [https://www.ebi.ac.uk/pdbsum/2ixn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ixn ProSAT]</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=2ixn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ixn OCA], [https://pdbe.org/2ixn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ixn RCSB], [https://www.ebi.ac.uk/pdbsum/2ixn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ixn ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/PTPA2_YEAST PTPA2_YEAST]] 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 TAP42-associated PP2A-like phosphatases modulating their activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex. Acts also inhibitory at high concentrations. Involved in the regulation of cell cycle progression, mitotic spindle formation and bud morphogenesis.<ref>PMID:11262194</ref> <ref>PMID:11134337</ref> <ref>PMID:12952889</ref> <ref>PMID:15447631</ref> <ref>PMID:15689491</ref> <ref>PMID:16380387</ref>
[https://www.uniprot.org/uniprot/PTPA2_YEAST PTPA2_YEAST] 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 TAP42-associated PP2A-like phosphatases modulating their activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex. Acts also inhibitory at high concentrations. Involved in the regulation of cell cycle progression, mitotic spindle formation and bud morphogenesis.<ref>PMID:11262194</ref> <ref>PMID:11134337</ref> <ref>PMID:12952889</ref> <ref>PMID:15447631</ref> <ref>PMID:15689491</ref> <ref>PMID:16380387</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 18824]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Barford, D]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Goris, J]]
[[Category: Barford D]]
[[Category: Jordens, J]]
[[Category: Goris J]]
[[Category: Leulliot, N]]
[[Category: Jordens J]]
[[Category: Quevillon-Cheruel, S]]
[[Category: Leulliot N]]
[[Category: Schiltz, M]]
[[Category: Quevillon-Cheruel S]]
[[Category: Tilbeurgh, H Van]]
[[Category: Schiltz M]]
[[Category: Vicentini, G]]
[[Category: Van Tilbeurgh H]]
[[Category: Isomerase]]
[[Category: Vicentini G]]
[[Category: Pp2a phosphatase activator prolyl isomerase ptpa]]