Structural insights into the enzymatic mechanism of the pathogenic MAPK phosphothreonine lyase.

Structural insights into the enzymatic mechanism of the pathogenic MAPK phosphothreonine lyase. Research Abstract Details 

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Structural insights into the enzymatic mechanism of the pathogenic MAPK phosphothreonine lyase. Abstract Text:

Yongqun Zhu,Hongtao Li,Chengzu Long,Liyan Hu,Hao Xu,Liping Liu,She Chen,Da-Cheng Wang,Feng Shao,Yongqun Zhu,Hongtao Li,Chengzu Long,Liyan Hu,Hao Xu,Liping Liu,She Chen,Da-Cheng Wang,Feng Shao,Yongqun Zhu,Hongtao Li,Chengzu Long,Liyan Hu,Hao Xu,Liping Liu,She Chen,Da-Cheng Wang,Feng Shao,

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.

Structural insights into the enzymatic mechanism of the pathogenic MAPK phosphothreonine lyase. Publishing Authors By Initials

Y Zhu,H Li,C Long,L Hu,H Xu,L Liu,S Chen,DC Wang,F Shao,Y Zhu,H Li,C Long,L Hu,H Xu,L Liu,S Chen,DC Wang,F Shao,Y Zhu,H Li,C Long,L Hu,H Xu,L Liu,S Chen,DC Wang,F Shao,

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Structural insights into the enzymatic mechanism of the pathogenic MAPK phosphothreonine lyase. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Molecular cell

VOLUME: 28

Page Numbers: 899-913

Journal Abbreviation: Mol. Cell

ISSN: 1097-2765

DAY: 29

MONTH: 11

YEAR: 2007

Structural insights into the enzymatic mechanism of the pathogenic MAPK phosphothreonine lyase. Information

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LANGUAGE: eng

NlmUniqueID: 9802571

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Grant and Affiliation Information for Structural insights into the enzymatic mechanism of the pathogenic MAPK phosphothreonine lyase.

AFFILIATION: National Institute of Biological Sciences, Beijing, 102206, China; National Laboratory of Macromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China.

Country: United States

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MEDLINETA: Mol Cell

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