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3c5w

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'''Complex between PP2A-specific methylesterase PME-1 and PP2A core enzyme'''
'''Complex between PP2A-specific methylesterase PME-1 and PP2A core enzyme'''
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==Overview==
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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.
==About this Structure==
==About this Structure==
3C5W is a [[Protein complex]] structure of sequences 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=3C5W OCA].
3C5W is a [[Protein complex]] structure of sequences 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=3C5W OCA].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/18394995 18394995]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Phosphatase]]
[[Category: Phosphatase]]
[[Category: Pp2a]]
[[Category: Pp2a]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 16 23:13:41 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 11 10:57:54 2008''

Revision as of 07:57, 11 June 2008

Image:3c5w.jpg

Template:STRUCTURE 3c5w

Complex between PP2A-specific methylesterase PME-1 and PP2A core enzyme


Overview

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.

About this Structure

3C5W is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Wed Jun 11 10:57:54 2008

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