5ELL

Crystal structure of L-aspartate/glutamate-specific racemase from Escherichia coli

5ELL の概要

• エントリーDOI: 10.2210/pdb5ell/pdb
• 関連するPDBエントリー: 5ELM
• 分子名称: Asp/Glu_racemase family protein (2 entities in total)
• 機能のキーワード: asp/glu racemase, l-form specific racemase, amino acid enantiomers, isomerase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 52810.25

構造登録者

Ahn, J.W.,Chang, J.H.,Kim, K.J. (登録日: 2015-11-04, 公開日: 2015-11-18, 最終更新日: 2023-11-08)

主引用文献

Ahn, J.W.,Chang, J.H.,Kim, K.J.
Structural basis for an atypical active site of an l-aspartate/glutamate-specific racemase from Escherichia coli
Febs Lett., 589:3842-3847, 2015

PubMed Abstract: We determined the crystal structure of EcL-DER to elucidate protein function and substrate specificity. Unlike other asp/glu racemases, EcL-DER has an unbalanced pair of catalytic residues, Thr83/Cys197, at the active site that is crucial for L- to D-unidirectional racemase activity. EcL-DER exhibited racemase activity for both L-glutamate and L-aspartate, but had threefold higher activity for L-glutamate. Based on the structure of the EcL-DER(C197S) mutant in complex with L-glutamate, we determined the binding mode of the L-glutamate substrate in EcL-DER and provide a structural basis for how the protein utilizes L-glutamate as a main substrate. The unidirectionality, despite an equilibrium constant of unity, can be understood in terms of the Haldane relationship.

PubMed: 26555188
DOI: 10.1016/j.febslet.2015.11.003

実験手法

X-RAY DIFFRACTION (1.801 Å)