Abstract
Homologs of the Escherichia coli surE gene are present in many eubacteria and archaea. Despite the evolutionary conservation, little information is available on the structure and function of their gene products. We have determined the crystal structure of the SurE protein from Thermotoga maritima. The structure reveals the dimeric arrangement of the subunits and an active site around a bound metal ion. We also demonstrate that the SurE protein exhibits a divalent metal ion-dependent phosphatase activity that is inhibited by vanadate or tungstate. In the vanadate- and tungstate-complexed structures, the inhibitors bind adjacent to the divalent metal ion. Our structural and functional analyses identify the SurE proteins as a novel family of metal ion-dependent phosphatases.
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Acknowledgements
We thank N. Sakabe and his staff for assistance during data collection at Photon Factory, beamline BL-18B. We also acknowledge the assistance of the staff at Pohang Light Source, beamline 6B and H.H. Lee. We thank the financial support from the Korea Science and Engineering Foundation (Basic Research Program grant no. 305-20000004). S.W.S. is supported by the BK21 program. J.E.K. is a recipient of the BK21 fellowship. J.M. is supported by the intern fellowship of KOSEF.
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Lee, J., Kwak, J., Moon, J. et al. Crystal structure and functional analysis of the SurE protein identify a novel phosphatase family. Nat Struct Mol Biol 8, 789–794 (2001). https://doi.org/10.1038/nsb0901-789
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DOI: https://doi.org/10.1038/nsb0901-789
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