Publication Abstract from PubMed
SurE is a stationary-phase survival protein found in bacteria, eukaryotes and archaea that exhibits a divalent-metal-ion-dependent phosphatase activity and acts as a nucleotidase and polyphosphate phosphohydrolase. The structure of the SurE protein from the hyperthermophile Aquifex aeolicus has been solved at 1.5 A resolution using molecular replacement with one dimer in the asymmetric unit and refined to an R factor of 15.6%. The crystal packing reveals that two dimers assemble to form a tetramer, although gel-filtration chromatography showed the presence of only a dimer in solution. The phosphatase active-site pocket was occupied by sulfate ions from the crystallization medium.
Structure of SurE protein from Aquifex aeolicus VF5 at 1.5 A resolution.,Antonyuk SV, Ellis MJ, Strange RW, Bessho Y, Kuramitsu S, Shinkai A, Yokoyama S, Hasnain SS Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Dec 1;65(Pt, 12):1204-8. Epub 2009 Nov 27. PMID:20054112[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
