2vep
From Proteopedia
CRYSTAL STRUCTURE OF THE FULL LENGTH BIFUNCTIONAL ENZYME PRIA
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. Arg19 and Ser81 were shown to play critical roles within the carboxyl and amino phosphate-binding sites, respectively; the catalytic residues Asp11 and Asp130 are responsible for both activities; and Thr166 and Asp171, 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. 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. 2008 Jan 4;365(1):16-21. Epub 2007 Oct 29. PMID:17967415 Page seeded by OCA on Sun May 4 18:40:39 2008
Categories: Single protein | Streptomyces coelicolor | Barona-Gomez, F. | Fulop, V. | Hodgson, D A. | Noda-Garcia, L. | Ochoa-Leyva, A. | Wright, H. | Amino-acid biosynthesis | Aromatic amino acid biosynthesis | Cytoplasm | Evolution of substrate specificity | Histidine biosynthesis | Isomerase | Pria | Tryptophan biosynthesis
