title: Crystal structure and functional analysis of the SurE protein identify a novel phosphatase family.
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.
authors.affiliation: School of Chemistry and Molecular Engineering, College of Natural Sciences, Seoul National University, Seoul 151-742, Korea.
authors.forename: J Y
authors.initials: JY
authors.lastname: Lee
authors.forename: J E
authors.initials: JE
authors.lastname: Kwak
authors.forename: J
authors.initials: J
authors.lastname: Moon
authors.forename: S H
authors.initials: SH
authors.lastname: Eom
authors.forename: E C
authors.initials: EC
authors.lastname: Liong
authors.forename: J D
authors.initials: JD
authors.lastname: Pedelacq
authors.forename: J
authors.initials: J
authors.lastname: Berendzen
authors.forename: S W
authors.initials: SW
authors.lastname: Suh
mesh_terms: D000135:Acid Phosphatase; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D001665:Binding Sites; D002413:Cations, Divalent / Q000378:metabolism; D018360:Crystallography, X-Ray; D029968:Escherichia coli Proteins; D008670:Metals / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009154:Mutation / Q000235:genetics; D010749:Phosphoprotein Phosphatases / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D020124:Thermotoga maritima / Q000201:enzymology* / Q000235:genetics; D017973:Tungsten Compounds / Q000378:metabolism / Q000494:pharmacology; D014638:Vanadates / Q000378:metabolism / Q000494:pharmacology
chemical_list: D001426:Bacterial Proteins; D002413:Cations, Divalent; D029968:Escherichia coli Proteins; D008670:Metals; D017973:Tungsten Compounds; D014638:Vanadates; D010749:Phosphoprotein Phosphatases; D000135:Acid Phosphatase; C089634:umpG protein, E coli; C045951:tungstate