Structural basis for the broad specificity of a new family of amino-acid racemases.
Acta Crystallogr D Biol Crystallogr
; 70(Pt 1): 79-90, 2014 Jan.
Article
in En
| MEDLINE
| ID: mdl-24419381
ABSTRACT
Broad-spectrum amino-acid racemases (Bsrs) enable bacteria to generate noncanonical D-amino acids, the roles of which in microbial physiology, including the modulation of cell-wall structure and the dissolution of biofilms, are just beginning to be appreciated. Here, extensive crystallographic, mutational, biochemical and bioinformatic studies were used to define the molecular features of the racemase BsrV that enable this enzyme to accommodate more diverse substrates than the related PLP-dependent alanine racemases. Conserved residues were identified that distinguish BsrV and a newly defined family of broad-spectrum racemases from alanine racemases, and these residues were found to be key mediators of the multispecificity of BrsV. Finally, the structural analysis of an additional Bsr that was identified in the bioinformatic analysis confirmed that the distinguishing features of BrsV are conserved among Bsr family members.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Vibrio cholerae
/
Amino Acid Isomerases
Language:
En
Journal:
Acta Crystallogr D Biol Crystallogr
Year:
2014
Type:
Article
Affiliation country:
Spain