1m3s
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Crystal structure of YckF from Bacillus subtilis
OverviewOverview
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.
About this StructureAbout this Structure
1M3S is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of Bacillus subtilis YckF: structural and functional evolution., Sanishvili R, Wu R, Kim DE, Watson JD, Collart F, Joachimiak A, J Struct Biol. 2004 Oct;148(1):98-109. PMID:15363790
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