5HQT

Crystal structure of an aspartate/glutamate racemase from Escherichia coli O157

Summary for 5HQT

• Entry DOI: 10.2210/pdb5hqt/pdb
• Related: 5HRA 5HRC
• Descriptor: aspartate/glutamate racemase, 2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID (3 entities in total)
• Functional Keywords: aspartate/glutamate racemase, plp-independent racemase, racemization mechanism, isomerase
• Biological source: Escherichia coli O157:H7 str. SS52
• Total number of polymer chains: 1
• Total formula weight: 26197.98

Authors

Liu, X.,Gao, F.,Ma, Y.,Liu, S.,Cui, Y.,Yuan, Z.,Kang, X. (deposition date: 2016-01-22, release date: 2016-04-20, Last modification date: 2023-11-08)

Primary citation

Liu, X.,Gao, F.,Ma, Y.,Liu, S.,Cui, Y.,Yuan, Z.,Kang, X.
Crystal structure and molecular mechanism of an aspartate/glutamate racemase from Escherichia coli O157
Febs Lett., 590:1262-1269, 2016

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.

PubMed: 27001440
DOI: 10.1002/1873-3468.12148

Experimental method

X-RAY DIFFRACTION (1.598 Å)