1jeo | pdb_00001jeo

File:1jeo.gif

spinqualitylabelsall models 1jeo, resolution 2.0Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D

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.

Overview

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).

About this Structure

1JEO is a Single protein structure of sequence from Methanocaldococcus jannaschii with CIT as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of MJ1247 protein from M. jannaschii at 2.0 A resolution infers a molecular function of 3-hexulose-6-phosphate isomerase., Martinez-Cruz LA, Dreyer MK, Boisvert DC, Yokota H, Martinez-Chantar ML, Kim R, Kim SH, Structure. 2002 Feb;10(2):195-204. PMID:11839305

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