Download MendeleyCrystal structure and molecular mechanism of an aspartate/glutamate racemase from Escherichia coli O157
Liu, X., Gao, F., Ma, Y., Liu, S., Cui, Y., Yuan, Z., Kang, X.(2016) FEBS Lett 590: 1262-1269
- PubMed: 27001440
- DOI: https://doi.org/10.1002/1873-3468.12148
- Primary Citation of Related Structures:
5HQT, 5HRA, 5HRC - PubMed Abstract:
EcL-DER, the aspartate/glutamate racemase from the pathogen Escherichia coli O157, exhibits racemase activity for l-aspartate and l-glutamate. This study reports the crystal structures of apo-EcL-DER, the EcL-DER-l-aspartate and the EcL-DER-d-aspartate complexes. The EcL-DER structure contains two domains, forming pseudo-mirror symmetry in the active site. A unique catalytic pair consisting of Thr(83) and Cys(197) exists in the active site. The characteristic conformations of l-Asp and d-Asp in the active site provide a straight structural evidence for the racemization mechanism of EcL-DER. In addition, the diversity of catalytic pairs implies that PLP-independent amino acid racemases adopt various catalytic mechanisms and are classified into different subgroups.
Organizational Affiliation:
College of Life Sciences, Hebei University, Baoding, China.
