The structure/function relationship of a dual-substrate (beta alpha)(8)-isomerase
Wright, Helena, Noda-Garcia, Lianet, Ochoa-Leyva, Adrian, Hodgson, D. A. (David A.), Fulop, Vilmos and Barona-Gomez, Francisco. (2008) The structure/function relationship of a dual-substrate (beta alpha)(8)-isomerase. Biochemical and Biophysical Research Communications, Vol.365 (No.1). pp. 16-21. ISSN 0006-291XFull text not available from this repository.
Official URL: http://dx.doi.org/10.1016/j.bbre.2007.10.101
Two structures of phosphoribosyl isomerase A (PriA) from Streptomyces coelicolor, involved in both histidine and tryptophan biosynthesis, were solved at 1.8 angstrom 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 (beta alpha)(8)-isomerase. (c) 2007 Elsevier Inc. All rights reserved.
|Item Type:||Journal Article|
|Subjects:||Q Science > QD Chemistry
Q Science > QH Natural history > QH301 Biology
|Divisions:||Faculty of Science > Life Sciences (2010- ) > Biological Sciences ( -2010)|
|Journal or Publication Title:||Biochemical and Biophysical Research Communications|
|Date:||4 January 2008|
|Number of Pages:||6|
|Page Range:||pp. 16-21|
|Access rights to Published version:||Restricted or Subscription Access|
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