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Structural basis for the catalytic mechanism of phosphothreonine lyase

Nature Structural & Molecular Biology volume 15, pages 101–102 (2008)Cite this article

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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Figure 1: Structures of free SpvC and its complex with a doubly phosphorylated peptide.
Figure 2: Substrate-induced conformational changes in SpvC result in complete sequestration of phosphothreonine.

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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.

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Author notes

  1. Linjie Chen and Huayi Wang: These authors contributed equally to this work.

Authors and 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, 94143-2550, California, USA

    Niu Huang

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  1. Linjie Chen
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Correspondence to Jijie Chai.

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Supplementary Figures 1–3, Supplementary Table 1, Supplementary Methods (PDF 1747 kb)

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Chen, L., Wang, H., Zhang, J. et al. Structural basis for the catalytic mechanism of phosphothreonine lyase. Nat Struct Mol Biol 15, 101–102 (2008). https://doi.org/10.1038/nsmb1329

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