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International Union of Crystallography, Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 12(65), p. 1204-1208, 2009

DOI: 10.1107/s1744309109043814

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Structure of SurE protein fromAquifex aeolicusVF5 at 1.5 Å resolution

Journal article published in 2009 by Svetlana V. Antonyuk ORCID, Mark J. Ellis, Richard W. Strange, Yoshitaka Bessho, Seiki Kuramitsu, Akeo Shinkai, Shigeyuki Yokoyama, S. Samar Hasnain
This paper was not found in any repository, but could be made available legally by the author.
This paper was not found in any repository, but could be made available legally by the author.

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Abstract

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.