嗜热栖热菌VF5来源的SurE蛋白在1.5埃分辨率下的结构
Structure of SurE protein from Aquifex aeolicus VF5 at 1.5 A resolution.
作者信息
Antonyuk Svetlana V, Ellis Mark J, Strange Richard W, Bessho Yoshitaka, Kuramitsu Seiki, Shinkai Akeo, Yokoyama Shigeyuki, Hasnain S Samar
机构信息
Molecular Biophysics Group, School of Biological Sciences, University of Liverpool, Crown Street, Liverpool L69 7ZB, England.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Dec 1;65(Pt 12):1204-8. doi: 10.1107/S1744309109043814. Epub 2009 Nov 27.
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.
SurE是一种在细菌、真核生物和古细菌中发现的稳定期存活蛋白，具有二价金属离子依赖性磷酸酶活性，可作为核苷酸酶和多磷酸磷酸水解酶。嗜热栖热菌（Aquifex aeolicus）的SurE蛋白结构已通过分子置换法以1.5埃的分辨率解析，不对称单元中有一个二聚体，并精修至R因子为15.6%。晶体堆积显示两个二聚体组装形成一个四聚体，尽管凝胶过滤色谱显示溶液中仅存在一个二聚体。磷酸酶活性位点口袋被来自结晶介质的硫酸根离子占据。
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