3VOT

Crystal structure of L-amino acid ligase from Bacillus licheniformis

3VOT の概要

• エントリーDOI: 10.2210/pdb3vot/pdb
• 分子名称: L-amino acid ligase, BL00235, ADENOSINE-5'-DIPHOSPHATE, CALCIUM ION, ... (6 entities in total)
• 機能のキーワード: atp-grasp motif, ligase, atp-binding
• 由来する生物種: Bacillus licheniformis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 96740.20

構造登録者

Suzuki, M.,Takahashi, Y.,Noguchi, A.,Arai, T.,Yagasaki, M.,Kino, K.,Saito, J. (登録日: 2012-02-08, 公開日: 2012-11-07, 最終更新日: 2024-03-20)

主引用文献

Suzuki, M.,Takahashi, Y.,Noguchi, A.,Arai, T.,Yagasaki, M.,Kino, K.,Saito, J.
The structure of L-amino-acid ligase from Bacillus licheniformis
Acta Crystallogr.,Sect.D, 68:1535-1540, 2012

PubMed Abstract: L-Amino-acid ligases (LALs) are enzymes which catalyze the formation of dipeptides by linking two L-amino acids. Although many dipeptides are known and expected to have medical and nutritional benefits, their practical use has been limited owing to their low availability and high expense. LALs are potentially desirable tools for the efficient production of dipeptides; however, the molecular basis of substrate recognition by LAL has not yet been sufficiently elucidated for the design of ideal LALs for the desired dipeptides. This report presents the crystal structure of the LAL BL00235 derived from Bacillus licheniformis NBRC 12200 determined at 1.9 Å resolution using the multi-wavelength anomalous dispersion method. The overall structure of BL00235 is fairly similar to that of YwfE, the only LAL with a known structure, but the structure around the catalytic site contains some significant differences. Detailed structural comparison of BL00235 with YwfE sheds some light on the molecular basis of the substrate specificities.

PubMed: 23090402
DOI: 10.1107/S0907444912038103

実験手法

X-RAY DIFFRACTION (1.8 Å)