2vep | pdb_00002vep

CRYSTAL STRUCTURE OF THE FULL LENGTH BIFUNCTIONAL ENZYME PRIA

File:2vep.gif

spinqualitylabelsall models 2vep, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D

Overview

Two structures of phosphoribosyl isomerase A (PriA) from Streptomyces, coelicolor, involved in both histidine and tryptophan biosynthesis, were, solved at 1.8A resolution. A closed conformer was obtained, which, represents the first complete structure of PriA, revealing hitherto, unnoticed molecular interactions and the occurrence of conformational, changes. Inspection of these conformers, including ligand-docking, simulations, allowed identification of residues involved in substrate, recognition, chemical catalysis and conformational changes. These, predictions were validated by mutagenesis and functional analysis. Arg(19), and Ser(81) were shown to play critical roles within the carboxyl and, amino phosphate-binding sites, respectively; the catalytic residues, Asp(11) and Asp(130) are responsible for both activities; and Thr(166) and, Asp(171), which make an unusual contact, are likely to elicit the, conformational changes needed for adopting the active site architectures., This represents the first report of the structure/function relationship of, this (betaalpha)(8)-isomerase.

About this Structure

2VEP is a Single protein structure of sequence from Streptomyces coelicolor with SO4 as ligand. Known structural/functional Sites: AC1 and AC2. Full crystallographic information is available from OCA.

Reference

The structure/function relationship of a dual-substrate (betaalpha)(8)-isomerase., Wright H, Noda-Garcia L, Ochoa-Leyva A, Hodgson DA, Fulop V, Barona-Gomez F, Biochem Biophys Res Commun. 2007 Oct 29;. PMID:17967415

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