Structure of SurE protein from Aquifex aeolicus VF5 at 1.5 A resolution.
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.
Antonyuk
Svetlana V
SV
Molecular Biophysics Group, School of Biological Sciences, University of Liverpool, Crown Street, Liverpool L69 7ZB, England.
Ellis
Mark J
MJ
Strange
Richard W
RW
Bessho
Yoshitaka
Y
Kuramitsu
Seiki
S
Shinkai
Akeo
A
Yokoyama
Shigeyuki
S
Hasnain
S Samar
SS
D000135:Acid Phosphatase / Q000737:chemistry; D001419:Bacteria / Q000737:chemistry* / Q000235:genetics; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D020134:Catalytic Domain; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray; D029968:Escherichia coli Proteins / Q000737:chemistry; D005798:Genes, Bacterial; D008958:Models, Molecular; D017510:Protein Folding; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D021122:Protein Subunits; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D055672:Static Electricity
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D021122:Protein Subunits; D011994:Recombinant Proteins; D000135:Acid Phosphatase; C089634:umpG protein, E coli