2VEP

Crystal Structure Of The Full Length Bifunctional Enzyme Pria

Summary for 2VEP

• Entry DOI: 10.2210/pdb2vep/pdb
• Related: 1VZW
• Descriptor: PHOSPHORIBOSYL ISOMERASE A, SULFATE ION (3 entities in total)
• Functional Keywords: aromatic amino acid biosynthesis, evolution of substrate specificity, tryptophan biosynthesis, histidine biosynthesis, amino-acid biosynthesis, pria, isomerase, (beta-alpha)8-barrel
• Biological source: STREPTOMYCES COELICOLOR
• Total number of polymer chains: 1
• Total formula weight: 25694.81

Authors

Wright, H.,Noda-Garcia, L.,Ochoa-Leyva, A.,Hodgson, D.A.,Fulop, V.,Barona-Gomez, F. (deposition date: 2007-10-25, release date: 2007-11-20, Last modification date: 2024-05-08)

Primary citation

Wright, H.,Noda-Garcia, L.,Ochoa-Leyva, A.,Hodgson, D.A.,Fulop, V.,Barona-Gomez, F.
The Structure/Function Relationship of a Dual Substrate (Betaalpha)(8)-Isomerase
Biochem.Biophys.Res.Commun., 365:16-, 2008

PubMed Abstract: 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.

PubMed: 17967415
DOI: 10.1016/J.BBRC.2007.10.101

Experimental method

X-RAY DIFFRACTION (1.8 Å)