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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Liu X,Gao F,Ma Y,Liu S,Cui Y,Yuan Z,Kang Xdoi
10.1002/1873-3468.12148subject
Has Abstractpub_date
2016-04-01 00:00:00pages
1262-9issue
8eissn
0014-5793issn
1873-3468journal_volume
590pub_type
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