4BHY

Structure of alanine racemase from Aeromonas hydrophila

Summary for 4BHY

• Entry DOI: 10.2210/pdb4bhy/pdb
• Descriptor: ALANINE RACEMASE (2 entities in total)
• Functional Keywords: isomerase, d-amino acids
• Biological source: AEROMONAS HYDROPHILA SUBSP. HYDROPHILA
• Total number of polymer chains: 4
• Total formula weight: 166018.11

Authors

Otero, L.H.,Carrasco-Lopez, C.,Bernardo-Garcia, N.,Hermoso, J.A. (deposition date: 2013-04-09, release date: 2014-01-15, Last modification date: 2023-12-20)

Primary citation

Espaillat, A.,Carrasco-Lopez, C.,Bernardo-Garcia, N.,Pietrosemoli, N.,Otero, L.H.,Alvarez, L.,De Pedro, M.A.,Pazos, F.,Davis, B.M.,Waldor, M.K.,Hermoso, J.A.,Cava, F.
Structural Basis for the Broad Specificity of a New Family of Amino-Acid Racemases.
Acta Crystallogr.,Sect.D, 70:79-, 2014

PubMed 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.

PubMed: 24419381
DOI: 10.1107/S1399004713024838

Experimental method

X-RAY DIFFRACTION (3.25 Å)