Structural basis for the broad specificity of a new family of amino-acid racemases
Entity
UAM. Departamento de Biología MolecularPublisher
International Union of CrystallographyDate
2014-01-01Citation
10.1107/S1399004713024838
Acta Crystallographica Section D: Biological Crystallography 70.1 (2014): 79-90
ISSN
0907-4449 (print); 1399-0047 (online)DOI
10.1107/S1399004713024838Funded by
Research in the Cava laboratory is supported by the MINECO, Spain (RYC-2010-06241), Universidad Autonoma de Madrid (UAM-38) and by the Knut and Alice Wallenberg Foundation (KAW). Additionally, this work was supported by the BFU2011-25326 MEC grant (JAH), by the S2010/BMD-2457 grant from CAM (JAH) and by HHMI (MKW)Project
Comunidad de Madrid. S2010/BMD-2457/BIPEDD2Editor's Version
http://dx.doi.org/10.1107/S1399004713024838Subjects
Amino-acid racemases; BsrV; Crystal structure; Multispecificity; Noncanonical d-amino acids; Biología y Biomedicina / BiologíaRights
© 2014 International Union of CrystallographyAbstract
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
Files in this item
Google Scholar:Espaillat, Akbar
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Carrasco-López, César
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Bernardo-García, Noelia
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Pietrosemoli, Natalia
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Otero, Lisandro H.
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Álvarez, Laura
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De Pedro, Miguel A.
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Pazos, Florencio
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Davis, Brigid M.
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Waldor, Matthew K.
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Hermoso, Juan A.
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Cava, Felipe
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