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2ixo

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Revision as of 21:30, 24 December 2014

CRYSTAL STRUCTURE OF THE PP2A PHOSPHATASE ACTIVATOR YPA1 PTPA1

Structural highlights

2ixo is a 2 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	2ixp
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[PTPA1_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. Involved in the regulation of cell cycle progression, mitotic spindle formation, bud morphogenesis and DNA repair.^[1] ^[2] ^[3] ^[4] ^[5] ^[6]

Evolutionary Conservation

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

Publication Abstract from PubMed

PTPA, an essential and specific activator of protein phosphatase 2A (PP2A), functions as a peptidyl prolyl isomerase (PPIase). We present here the crystal structures of human PTPA and of the two yeast orthologs (Ypa1 and Ypa2), revealing an all alpha-helical protein fold that is radically different from other PPIases. The protein is organized into two domains separated by a groove lined by highly conserved residues. To understand the molecular mechanism of PTPA activity, Ypa1 was cocrystallized with a proline-containing PPIase peptide substrate. In the complex, the peptide binds at the interface of a peptide-induced dimer interface. Conserved residues of the interdomain groove contribute to the peptide binding site and dimer interface. Structure-guided mutational studies showed that in vivo PTPA activity is influenced by mutations on the surface of the peptide binding pocket, the same mutations that also influenced the in vitro activation of PP2Ai and PPIase activity.

Crystal structure of the PP2A phosphatase activator: implications for its PP2A-specific PPIase activity.,Leulliot N, Vicentini G, Jordens J, Quevillon-Cheruel S, Schiltz M, Barford D, van Tilbeurgh H, Goris J Mol Cell. 2006 Aug 4;23(3):413-24. PMID:16885030^[7]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Van Hoof C, Janssens V, De Baere I, Stark MJ, de Winde JH, Winderickx J, Thevelein JM, Merlevede W, Goris J. The Saccharomyces cerevisiae phosphotyrosyl phosphatase activator proteins are required for a subset of the functions disrupted by protein phosphatase 2A mutations. Exp Cell Res. 2001 Apr 1;264(2):372-87. PMID:11262194 doi:http://dx.doi.org/10.1006/excr.2000.5144
↑ Mitchell DA, Sprague GF Jr. The phosphotyrosyl phosphatase activator, Ncs1p (Rrd1p), functions with Cla4p to regulate the G(2)/M transition in Saccharomyces cerevisiae. Mol Cell Biol. 2001 Jan;21(2):488-500. PMID:11134337 doi:http://dx.doi.org/10.1128/MCB.21.2.488-500.2001
↑ Fellner T, Lackner DH, Hombauer H, Piribauer P, Mudrak I, Zaragoza K, Juno C, Ogris E. A novel and essential mechanism determining specificity and activity of protein phosphatase 2A (PP2A) in vivo. Genes Dev. 2003 Sep 1;17(17):2138-50. PMID:12952889 doi:http://dx.doi.org/10.1101/gad.259903
↑ Douville J, David J, Fortier PK, Ramotar D. The yeast phosphotyrosyl phosphatase activator protein, yPtpa1/Rrd1, interacts with Sit4 phosphatase to mediate resistance to 4-nitroquinoline-1-oxide and UVA. Curr Genet. 2004 Aug;46(2):72-81. Epub 2004 May 19. PMID:15150670 doi:http://dx.doi.org/10.1007/s00294-004-0513-9
↑ Zheng Y, Jiang Y. The yeast phosphotyrosyl phosphatase activator is part of the Tap42-phosphatase complexes. Mol Biol Cell. 2005 Apr;16(4):2119-27. Epub 2005 Feb 2. PMID:15689491 doi:http://dx.doi.org/E04-09-0797
↑ Jordens J, Janssens V, Longin S, Stevens I, Martens E, Bultynck G, Engelborghs Y, Lescrinier E, Waelkens E, Goris J, Van Hoof C. The protein phosphatase 2A phosphatase activator is a novel peptidyl-prolyl cis/trans-isomerase. J Biol Chem. 2006 Mar 10;281(10):6349-57. Epub 2005 Dec 27. PMID:16380387 doi:http://dx.doi.org/M507760200
↑ Leulliot N, Vicentini G, Jordens J, Quevillon-Cheruel S, Schiltz M, Barford D, van Tilbeurgh H, Goris J. Crystal structure of the PP2A phosphatase activator: implications for its PP2A-specific PPIase activity. Mol Cell. 2006 Aug 4;23(3):413-24. PMID:16885030 doi:10.1016/j.molcel.2006.07.008

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2ixo"

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[2ixo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IXO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2IXO FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ixp|2ixp]]</td></tr>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ixp|2ixp]]</td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ixo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ixo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ixo RCSB], [http://www.ebi.ac.uk/pdbsum/2ixo PDBsum]</span></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=2ixo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ixo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ixo RCSB], [http://www.ebi.ac.uk/pdbsum/2ixo PDBsum]</span></td></tr>
-<table>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/PTPA1_YEAST PTPA1_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. Involved in the regulation of cell cycle progression, mitotic spindle formation, bud morphogenesis and DNA repair.<ref>PMID:11262194</ref> <ref>PMID:11134337</ref> <ref>PMID:12952889</ref> <ref>PMID:15150670</ref> <ref>PMID:15689491</ref> <ref>PMID:16380387</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 29: / Line 31: @@
 </StructureSection>
 [[Category: Saccharomyces cerevisiae]]
-[[Category: Barford, D.]]
+[[Category: Barford, D]]
-[[Category: Goris, J.]]
+[[Category: Goris, J]]
-[[Category: Jordens, J.]]
+[[Category: Jordens, J]]
-[[Category: Leulliot, N.]]
+[[Category: Leulliot, N]]
-[[Category: Quevillon-Cheruel, S.]]
+[[Category: Quevillon-Cheruel, S]]
-[[Category: Schiltz, M.]]
+[[Category: Schiltz, M]]
-[[Category: Tilbeurgh, H Van.]]
+[[Category: Tilbeurgh, H Van]]
-[[Category: Vicentini, G.]]
+[[Category: Vicentini, G]]
 [[Category: Isomerase]]
 [[Category: Nuclear protein]]
 [[Category: Pp2a phosphatase activator prolyl isomerase ptpa]]

2ixo

From Proteopedia

Revision as of 21:30, 24 December 2014

CRYSTAL STRUCTURE OF THE PP2A PHOSPHATASE ACTIVATOR YPA1 PTPA1

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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