Crystal structure and functional analysis of the SurE protein identify a novel phosphatase family

被引:0
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作者
Jae Young Lee
Jae Eun Kwak
Jinho Moon
Soo Hyun Eom
Elaine C. Liong
Jean-Denis Pedelacq
Joel Berendzen
Se Won Suh
机构
[1] School of Chemistry and Molecular Engineering,Department of Life Science
[2] College of Natural Sciences,undefined
[3] Seoul National University,undefined
[4] Kwangju Institute of Science and Technology,undefined
[5] Biophysics Group,undefined
[6] Los Alamos National Laboratory,undefined
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摘要
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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页码:789 / 794
页数:5
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