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Journal of Bacteriology, February 2006, p. 1509-1517, Vol. 188, No. 4
0021-9193/06/$08.00+0     doi:10.1128/JB.188.4.1509-1517.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Solution Structure of a Low-Molecular-Weight Protein Tyrosine Phosphatase from Bacillus subtilis

Huimin Xu,1,2 Bin Xia,1,2,3 and Changwen Jin1,2,3*

Beijing Nuclear Magnetic Resonance Center,1 College of Life Sciences,2 College of Chemistry and Molecular Engineering, Peking University, Beijing 100871, China3

Received 18 July 2005/ Accepted 14 November 2005

The low-molecular-weight (LMW) protein tyrosine phosphatases (PTPs) exist ubiquitously in prokaryotes and eukaryotes and play important roles in cellular processes. We report here the solution structure of YwlE, an LMW PTP identified from the gram-positive bacteria Bacillus subtilis. YwlE consists of a twisted central four-stranded parallel ß-sheet with seven {alpha}-helices packing on both sides. Similar to LMW PTPs from other organisms, the conformation of the YwlE active site is favorable for phosphotyrosine binding, indicating that it may share a common catalytic mechanism in the hydrolysis of phosphate on tyrosine residue in proteins. Though the overall structure resembles that of the eukaryotic LMW PTPs, significant differences were observed around the active site. Residue Asp115 is likely interacting with residue Arg13 through electrostatic interaction or hydrogen bond interaction to stabilize the conformation of the active cavity, which may be a unique character of bacterial LMW PTPs. Residues in the loop region from Phe40 to Thr48 forming a wall of the active cavity are more flexible than those in other regions. Ala41 and Gly45 are located near the active cavity and form a noncharged surface around it. These unique properties demonstrate that this loop may be involved in interaction with specific substrates. In addition, the results from spin relaxation experiments elucidate further insights into the mobility of the active site. The solution structure in combination with the backbone dynamics provides insights into the mechanism of substrate specificity of bacterial LMW PTPs.

* Corresponding author. Mailing address: Beijing Nuclear Magnetic Resonance Center, Peking University, Beijing 100871, China. Phone: 86-10-6275-6004. Fax: 86-10-6275-3790. E-mail: changwen{at}pku.edu.cn.

Journal of Bacteriology, February 2006, p. 1509-1517, Vol. 188, No. 4
0021-9193/06/$08.00+0     doi:10.1128/JB.188.4.1509-1517.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Lescop, E., Hu, Y., Xu, H., Hu, W., Chen, J., Xia, B., Jin, C. (2006). The Solution Structure of Escherichia coli Wzb Reveals a Novel Substrate Recognition Mechanism of Prokaryotic Low Molecular Weight Protein-tyrosine Phosphatases. J. Biol. Chem. 281: 19570-19577 [Abstract] [Full Text]  


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