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Structural basis for the broad specificity of a new family of amino-acid racemases

AutorEspaillat, Akbar; Álvarez, Laura ; Pedro, Miguel Ángel de ; Cava, Felipe
Fecha de publicaciónjun-2014
EditorBlackwell Publishing
CitaciónActa Crystallographica Section D: Biological Crystallography 70: 79- 90 (2014)
ResumenBroad-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. © 2014 International Union of Crystallography.
URIhttp://hdl.handle.net/10261/125535
DOI10.1107/S1399004713024838
Identificadoresdoi: 10.1107/S1399004713024838
issn: 0907-4449
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