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3c5v

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Revision as of 05:06, 16 November 2017

PP2A-specific methylesterase apo form (PME)

Structural highlights

3c5v is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	3c5w
Gene:	PPME1, PME1 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PPME1_HUMAN] Demethylates proteins that have been reversibly carboxymethylated. Demethylates PPP2CB (in vitro) and PPP2CA. Binding to PPP2CA displaces the manganese ion and inactivates the enzyme.^[1]

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

Protein phosphatase 2A (PP2A) is an important serine/threonine phosphatase that plays a role in many biological processes. Reversible carboxyl methylation of the PP2A catalytic subunit is an essential regulatory mechanism for its function. Demethylation and negative regulation of PP2A is mediated by a PP2A-specific methylesterase PME-1, which is conserved from yeast to humans. However, the underlying mechanism of PME-1 function remains enigmatic. Here we report the crystal structures of PME-1 by itself and in complex with a PP2A heterodimeric core enzyme. The structures reveal that PME-1 directly binds to the active site of PP2A and that this interaction results in the activation of PME-1 by rearranging the catalytic triad into an active conformation. Strikingly, these interactions also lead to inactivation of PP2A by evicting the manganese ions that are required for the phosphatase activity of PP2A. These observations identify a dual role of PME-1 that regulates PP2A activation, methylation, and holoenzyme assembly in cells.

Structural mechanism of demethylation and inactivation of protein phosphatase 2A.,Xing Y, Li Z, Chen Y, Stock JB, Jeffrey PD, Shi Y Cell. 2008 Apr 4;133(1):154-63. PMID:18394995^[2]

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

References

↑ Ogris E, Du X, Nelson KC, Mak EK, Yu XX, Lane WS, Pallas DC. A protein phosphatase methylesterase (PME-1) is one of several novel proteins stably associating with two inactive mutants of protein phosphatase 2A. J Biol Chem. 1999 May 14;274(20):14382-91. PMID:10318862
↑ Xing Y, Li Z, Chen Y, Stock JB, Jeffrey PD, Shi Y. Structural mechanism of demethylation and inactivation of protein phosphatase 2A. Cell. 2008 Apr 4;133(1):154-63. PMID:18394995 doi:http://dx.doi.org/10.1016/j.cell.2008.02.041

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/3c5v"

@@ Line 1: / Line 1: @@
 ==PP2A-specific methylesterase apo form (PME)==
 <StructureSection load='3c5v' size='340' side='right' caption='[[3c5v]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3c5w|3c5w]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PPME1, PME1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3c5v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c5v OCA], [http://pdbe.org/3c5v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3c5v RCSB], [http://www.ebi.ac.uk/pdbsum/3c5v 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=3c5v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c5v OCA], [http://pdbe.org/3c5v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3c5v RCSB], [http://www.ebi.ac.uk/pdbsum/3c5v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3c5v ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 28: / Line 29: @@
 </div>
 <div class="pdbe-citations 3c5v" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Methylesterase|Methylesterase]]
 == References ==
 <references/>
@@ Line 42: / Line 40: @@
 [[Category: Stock, J]]
 [[Category: Xing, Y]]
+[[Category: Alternative splicing]]
 [[Category: Demethylase]]
 [[Category: Hydrolase]]

3c5v

From Proteopedia

Revision as of 05:06, 16 November 2017

PP2A-specific methylesterase apo form (PME)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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