Crystal structure of Bacillus subtilis YckF: structural and functional evolution

Journal of Structural Biology
Ruslan SanishviliAndrzej Joachimiak

Abstract

The crystal structure of the YckF protein from Bacillus subtilis was determined with MAD phasing and refined at 1.95A resolution. YckF forms a tight tetramer both in crystals and in solution. Conservation of such oligomerization in other phosphate sugar isomerases indicates that the crystallographically observed tetramer is physiologically relevant. The structure of YckF was compared to with its ortholog from Methanococcus jannaschii, MJ1247. Both of these proteins have phosphate hexulose isomerase activity, although neither of the organisms can utilize methane or methanol as source of energy and/or carbon. Extensive sequence and structural similarities with MJ1247 and with the isomerase domain of glucosamine-6-phosphate synthase from Escherichia coli allowed us to group residues contributing to substrate binding or catalysis. Few notable differences among these structures suggest possible cooperativity of the four active sites of the tetramer. Phylogenetic relationships between obligatory and facultative methylotrophs along with B. subtilis and E. coli provide clues about the possible evolution of genes as they loose their physiological importance.

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Citations

Jul 14, 2009·Applied Microbiology and Biotechnology·Hiroya YurimotoYasuyoshi Sakai
Oct 31, 2007·Journal of Structural and Functional Genomics·Tatiana PetrovaAndrzej Joachimiak
Aug 12, 2009·Biochemical and Biophysical Research Communications·Silvia SommarugaAlessandra Polissi
Sep 25, 2018·Chembiochem : a European Journal of Chemical Biology·Liwen FanYanhe Ma
Aug 17, 2006·Critical Reviews in Biochemistry and Molecular Biology·Eric M Phizicky, Elizabeth J Grayhack

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