3VOT

Crystal structure of L-amino acid ligase from Bacillus licheniformis

Summary for 3VOT

• Entry DOI: 10.2210/pdb3vot/pdb
• Descriptor: L-amino acid ligase, BL00235, ADENOSINE-5'-DIPHOSPHATE, CALCIUM ION, ... (6 entities in total)
• Functional Keywords: atp-grasp motif, ligase, atp-binding
• Biological source: Bacillus licheniformis
• Total number of polymer chains: 2
• Total formula weight: 96740.20

Authors

Suzuki, M.,Takahashi, Y.,Noguchi, A.,Arai, T.,Yagasaki, M.,Kino, K.,Saito, J. (deposition date: 2012-02-08, release date: 2012-11-07, Last modification date: 2024-03-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.8 Å)