1mkp
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The crystal structure of the catalytic domain from the MAPK phosphatase | + | The crystal structure of the catalytic domain from the MAPK phosphatase Pyst1 (Pyst1-CD) has been determined at 2.35 A. The structure adopts a protein tyrosine phosphatase (PTPase) fold with a shallow active site that displays a distorted geometry in the absence of its substrate with some similarity to the dual-specificity phosphatase cdc25. Functional characterization of Pyst1-CD indicates it is sufficient to dephosphorylate activated ERK2 in vitro. Kinetic analysis of Pyst1 and Pyst1-CD using the substrate p-nitrophenyl phosphate (pNPP) reveals that both molecules undergo catalytic activation in the presence of recombinant inactive ERK2, switching from a low- to high-activity form. Mutation of Asp 262, located 5.5 A distal to the active site, demonstrates it is essential for catalysis in the high-activity ERK2-dependent conformation of Pyst1 but not for the low-activity ERK2-independent form, suggesting that ERK2 induces closure of the Asp 262 loop over the active site, thereby enhancing Pyst1 catalytic efficiency. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Dowd, S.]] | [[Category: Dowd, S.]] | ||
[[Category: Keyse, S.]] | [[Category: Keyse, S.]] | ||
| - | [[Category: Mcdonald, N | + | [[Category: Mcdonald, N Q.]] |
| - | [[Category: Stewart, A | + | [[Category: Stewart, A E.]] |
[[Category: CL]] | [[Category: CL]] | ||
[[Category: MPD]] | [[Category: MPD]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:56:11 2008'' |
Revision as of 11:56, 21 February 2008
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CRYSTAL STRUCTURE OF PYST1 (MKP3)
Overview
The crystal structure of the catalytic domain from the MAPK phosphatase Pyst1 (Pyst1-CD) has been determined at 2.35 A. The structure adopts a protein tyrosine phosphatase (PTPase) fold with a shallow active site that displays a distorted geometry in the absence of its substrate with some similarity to the dual-specificity phosphatase cdc25. Functional characterization of Pyst1-CD indicates it is sufficient to dephosphorylate activated ERK2 in vitro. Kinetic analysis of Pyst1 and Pyst1-CD using the substrate p-nitrophenyl phosphate (pNPP) reveals that both molecules undergo catalytic activation in the presence of recombinant inactive ERK2, switching from a low- to high-activity form. Mutation of Asp 262, located 5.5 A distal to the active site, demonstrates it is essential for catalysis in the high-activity ERK2-dependent conformation of Pyst1 but not for the low-activity ERK2-independent form, suggesting that ERK2 induces closure of the Asp 262 loop over the active site, thereby enhancing Pyst1 catalytic efficiency.
About this Structure
1MKP is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of the MAPK phosphatase Pyst1 catalytic domain and implications for regulated activation., Stewart AE, Dowd S, Keyse SM, McDonald NQ, Nat Struct Biol. 1999 Feb;6(2):174-81. PMID:10048930
Page seeded by OCA on Thu Feb 21 13:56:11 2008
Categories: Homo sapiens | Single protein | Dowd, S. | Keyse, S. | Mcdonald, N Q. | Stewart, A E. | CL | MPD | Hydrolase
