2q8y
From Proteopedia
(New page: 200px<br /><applet load="2q8y" size="350" color="white" frame="true" align="right" spinBox="true" caption="2q8y, resolution 2.00Å" /> '''Structural insight i...) |
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==Overview== | ==Overview== | ||
| - | The OspF family of phosphothreonine lyase, including SpvC from Salmonella, irreversibly inactivates the dual-phosphorylated host MAPKs (pT-X-pY) | + | The OspF family of phosphothreonine lyase, including SpvC from Salmonella, irreversibly inactivates the dual-phosphorylated host MAPKs (pT-X-pY) through beta elimination. We determined crystal structures of SpvC and its complex with a phosphopeptide substrate. SpvC adopts a unique fold of alpha/beta type. The disordered N terminus harbors a canonical D motif for MAPK substrate docking. The enzyme-substrate complex structure indicates that recognition of the phosphotyrosine followed by insertion of the threonine phosphate into an arginine pocket places the phosphothreonine into the enzyme active site. This requires the conformational flexibility of pT-X-pY, which suggests that p38 (pT-G-pY) is likely the preferred physiological substrate. Structure-based biochemical and enzymatic analysis allows us to propose a general acid/base mechanism for beta elimination reaction catalyzed by the phosphothreonine lyase. The mechanism described here provides a structural understanding of MAPK inactivation by a family of pathogenic effectors conserved in plant and animal systems and may also open a new route for biological catalysis. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Salmonella enteritidis]] | [[Category: Salmonella enteritidis]] | ||
[[Category: Shao, F.]] | [[Category: Shao, F.]] | ||
| - | [[Category: Wang, D | + | [[Category: Wang, D C.]] |
| - | [[Category: Zhu, Y | + | [[Category: Zhu, Y Q.]] |
[[Category: alpha/beta fold]] | [[Category: alpha/beta fold]] | ||
[[Category: lyase/transferase complex]] | [[Category: lyase/transferase complex]] | ||
| - | ''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 18:37:15 2008'' |
Revision as of 16:37, 21 February 2008
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Structural insight into the enzymatic mechanism of the phophothreonine lyase
Overview
The OspF family of phosphothreonine lyase, including SpvC from Salmonella, irreversibly inactivates the dual-phosphorylated host MAPKs (pT-X-pY) through beta elimination. We determined crystal structures of SpvC and its complex with a phosphopeptide substrate. SpvC adopts a unique fold of alpha/beta type. The disordered N terminus harbors a canonical D motif for MAPK substrate docking. The enzyme-substrate complex structure indicates that recognition of the phosphotyrosine followed by insertion of the threonine phosphate into an arginine pocket places the phosphothreonine into the enzyme active site. This requires the conformational flexibility of pT-X-pY, which suggests that p38 (pT-G-pY) is likely the preferred physiological substrate. Structure-based biochemical and enzymatic analysis allows us to propose a general acid/base mechanism for beta elimination reaction catalyzed by the phosphothreonine lyase. The mechanism described here provides a structural understanding of MAPK inactivation by a family of pathogenic effectors conserved in plant and animal systems and may also open a new route for biological catalysis.
About this Structure
2Q8Y is a Protein complex structure of sequences from Salmonella enteritidis. Active as Lyase, with EC number 4.2. Full crystallographic information is available from OCA.
Reference
Structural insights into the enzymatic mechanism of the pathogenic MAPK phosphothreonine lyase., Zhu Y, Li H, Long C, Hu L, Xu H, Liu L, Chen S, Wang DC, Shao F, Mol Cell. 2007 Dec 14;28(5):899-913. Epub 2007 Nov 29. PMID:18060821
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