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Structural basis for the catalytic mechanism of phosphothreonine lyase

Nature Structural & Molecular Biology volume 15, pages 101102 (2008) | Download Citation

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Abstract

Salmonella SpvC belongs to a new enzyme family designated phosphothreonine lyases that irreversibly inactivate mitogen-activated protein kinases. The crystal structure of SpvC reported here reveals that the two phosphorylated residues in the substrate peptide predominantly mediate its recognition by SpvC. Substrate-induced conformational changes in SpvC sequester the phosphothreonine in a completely solvent-free environment, preventing the hydrolysis of the phosphate group and facilitating the elimination reaction.

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Acknowledgements

We thank Y. Dong and P. Liu at the Beijing Synchrotron Radiation Facility for assistance with the data collection. This research is funded by Chinese Ministry of Science and Technology '863' grants 2003-AA210090 to J.C. and 2003-AA210080 to J.Z.

Author information

Author notes

    • Linjie Chen
    •  & Huayi Wang

    These authors contributed equally to this work.

Affiliations

  1. Graduate Program in Chinese Academy of Medical Sciences and Beijing Union Medical College, Beijing 100730, China.

    • Linjie Chen
    •  & Huayi Wang
  2. National Institute of Biological Sciences, Beijing 102206, China.

    • Linjie Chen
    • , Huayi Wang
    • , Jie Zhang
    • , Niu Huang
    • , Jian-Min Zhou
    •  & Jijie Chai
  3. State Key Lab of Microbial Technology, Shandong University, Jinan 250100, China.

    • Lichuan Gu
  4. Department of Pharmaceutical Chemistry, University of California San Francisco, QB3 Building, 1700 Fourth Street, Box 2550, San Francisco, California 94143-2550, USA.

    • Niu Huang

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Corresponding author

Correspondence to Jijie Chai.

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    Supplementary Text and Figures

    Supplementary Figures 1–3, Supplementary Table 1, Supplementary Methods

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DOI

https://doi.org/10.1038/nsmb1329