5HQT: Crystal Structure Of An Aspartate/glutamate Racemase From Escherichia Coli O157

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.
PDB ID: 5HQTDownload
MMDB ID: 139430
PDB Deposition Date: 2016/1/22
Updated in MMDB: 2016/05
Experimental Method:
x-ray diffraction
Resolution: 1.6  Å
Source Organism:
Similar Structures:
Biological Unit for 5HQT: dimeric; determined by author and by software (PISA)
Molecular Components in 5HQT
Label Count Molecule
Proteins (2 molecules)
Aspartate/glutamate Racemase
Molecule annotation
Chemicals (2 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB