3c5v
From Proteopedia
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'''PP2A-specific methylesterase apo form (PME)''' | '''PP2A-specific methylesterase apo form (PME)''' | ||
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| + | ==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== | ==About this Structure== | ||
3C5V is a [[Single protein]] structure of sequence 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=3C5V OCA]. | 3C5V is a [[Single protein]] structure of sequence 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=3C5V OCA]. | ||
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| + | ==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:[http://www.ncbi.nlm.nih.gov/pubmed/18394995 18394995] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Pp2a]] | [[Category: Pp2a]] | ||
[[Category: Serine esterase]] | [[Category: Serine esterase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 11 10:57:53 2008'' |
Revision as of 07:57, 11 June 2008
PP2A-specific methylesterase apo form (PME)
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
3C5V is a Single protein structure of sequence 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 10:57:53 2008
Categories: Homo sapiens | Single protein | Chen, Y. | Jeffrey, P D. | Li, Z. | Shi, Y. | Stock, J. | Xing, Y. | Alternative splicing | Demethylase | Hydrolase | Phosphoprotein | Pp2a | Serine esterase
