Structural highlights
Function
SURE_AQUAE Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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.
References
- ↑ Antonyuk SV, Ellis MJ, Strange RW, Bessho Y, Kuramitsu S, Shinkai A, Yokoyama S, Hasnain SS. Structure of SurE protein from Aquifex aeolicus VF5 at 1.5 A resolution. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Dec 1;65(Pt, 12):1204-8. Epub 2009 Nov 27. PMID:20054112 doi:10.1107/S1744309109043814
