1JEO

Crystal Structure of the Hypothetical Protein MJ1247 from Methanococcus jannaschii at 2.0 A Resolution Infers a Molecular Function of 3-Hexulose-6-Phosphate isomerase.

Summary for 1JEO

• Entry DOI: 10.2210/pdb1jeo/pdb
• Descriptor: HYPOTHETICAL PROTEIN MJ1247, CITRIC ACID (3 entities in total)
• Functional Keywords: rump pathway, phosphosugar, 3-hexulose-6-phosphate isomerase, phi, structural genomics, bsgc structure funded by nih, protein structure initiative, psi, berkeley structural genomics center, isomerase
• Biological source: Methanocaldococcus jannaschii
• Total number of polymer chains: 1
• Total formula weight: 20890.58

Authors

Martinez-Cruz, L.A.,Dreyer, M.K.,Boisvert, D.C.,Yokota, H.,Martinez-Chantar, M.L.,Kim, R.,Kim, S.H.,Berkeley Structural Genomics Center (BSGC) (deposition date: 2001-06-18, release date: 2002-02-20, Last modification date: 2024-11-20)

Primary citation

Martinez-Cruz, L.A.,Dreyer, M.K.,Boisvert, D.C.,Yokota, H.,Martinez-Chantar, M.L.,Kim, R.,Kim, S.H.
Crystal structure of MJ1247 protein from M. jannaschii at 2.0 A resolution infers a molecular function of 3-hexulose-6-phosphate isomerase.
Structure, 10:195-204, 2002

PubMed Abstract: The crystal structure of the hypothetical protein MJ1247 from Methanococccus jannaschii at 2 A 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 alpha 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).

PubMed: 11839305
DOI: 10.1016/S0969-2126(02)00701-3

Experimental method

X-RAY DIFFRACTION (2 Å)