Crystal structure and molecular mechanism of an aspartate/glutamate racemase from Escherichia coli O157.

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 Lett

journal_title

FEBS letters

authors

Liu X,Gao F,Ma Y,Liu S,Cui Y,Yuan Z,Kang X

doi

10.1002/1873-3468.12148

subject

Has Abstract

pub_date

2016-04-01 00:00:00

pages

1262-9

issue

8

eissn

0014-5793

issn

1873-3468

journal_volume

590

pub_type

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