Open AccessStructure of SurE protein from Aquifex aeolicus VF5 at 1.5 Å resolution
Author(s) -
Antonyuk Svetlana V.,
Ellis Mark J.,
Strange Richard W.,
Bessho Yoshitaka,
Kuramitsu Seiki,
Shinkai Akeo,
Yokoyama Shigeyuki,
Hasnain S. Samar
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109043814
Subject(s) - aquifex aeolicus , hyperthermophile , tetramer , crystallography , dimer , chemistry , polyphosphate , resolution (logic) , phosphatase , archaea , phosphate , biochemistry , escherichia coli , enzyme , organic chemistry , artificial intelligence , computer science , gene
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 Å 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.