Artículo
Structural basis for the broad specificity of a new family of amino-acid racemases
Espaillat, Akbar; Carrasco Lépez, Cesar; Bernardo García, Noelia; Pietrosemolli, Natalia; Otero, Lisandro Horacio
; Alvarez, Laura; de Pedro, Miguel A.; Pazos, Florencio; Davis, Brigid M.; Waldor, Matthew K.; Hermoso, Juan A.; Cava, Felipe
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Fecha de publicación:
01/2014
Editorial:
Wiley Blackwell Publishing, Inc
Revista:
Acta Crystallographica Section D-biological Crystallography
ISSN:
0907-4449
Idioma:
Inglés
Tipo de recurso:
Artículo publicado
Clasificación temática:
Resumen
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.
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Articulos(IIBBA)
Articulos de INST.DE INVEST.BIOQUIMICAS DE BS.AS(I)
Articulos de INST.DE INVEST.BIOQUIMICAS DE BS.AS(I)
Citación
Espaillat, Akbar; Carrasco Lépez, Cesar; Bernardo García, Noelia; Pietrosemolli, Natalia; Otero, Lisandro Horacio; et al.; Structural basis for the broad specificity of a new family of amino-acid racemases; Wiley Blackwell Publishing, Inc; Acta Crystallographica Section D-biological Crystallography; 70; Pt1; 1-2014; 79-90
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