Journal
STRUCTURE
Volume 10, Issue 2, Pages 195-204Publisher
CELL PRESS
DOI: 10.1016/S0969-2126(02)00701-3
Keywords
3-hexulose-6-phosphate isomerase; hypothetical protein function; Methanococcus jannaschii; phosphosugar; RuMP pathway; structural genomics
Funding
- NIGMS NIH HHS [P50GM62412] Funding Source: Medline
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The crystal structure of the hypothetical protein MJ1247 from Methanococccus jannaschii at 2 Angstrom resolution, a detailed sequence analysis, and biochemical assays infer its molecular function to be 3-hexulose-6-phosphate isomerase (PHI). In the dissimilatory ribulose monophosphate (RuMP) cycle, ribulose-5-phosphate is coupled to formaldehyde by the 3-hexulose-6-phosphate synthase (HPS), yielding hexulose-6-phosphate, which is then isomerized to fructose-6-phosphate by the enzyme 3-hexulose-6-phosphate isomerase. MJ1247 is an alpha/beta structure consisting of a five-stranded parallel beta sheet flanked on both sides by et helices, forming a three-layered alpha-beta-alpha sandwich. The fold represents the nucleotide binding motif of a flavodoxin type. MJ1247 is a tetramer in the crystal and in solution and each monomer has a folding similar to the isomerase domain of glucosamine-6-phosphate synthase (GlmS).
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