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

Jae Young Lee, Jae Eun Kwak, Jinho Moon, Soo Hyun Eom, Elaine C. Liong, Jean Denis Pedelacq, Joel Berendzen, Se Won Suh

Research output: Contribution to journalArticlepeer-review

42 Scopus citations

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.

Original languageEnglish
Pages (from-to)789-794
Number of pages6
JournalNature Structural Biology
Volume8
Issue number9
DOIs
StatePublished - 2001

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