Structure of RizA, an L-amino-acid ligase from Bacillus subtilis

Wataru Kagawa; Toshinobu Arai; Shun Ishikura; Kuniki Kino; Hitoshi Kurumizaka

doi:10.1107/S2053230X15012698

Structure of RizA, an L-amino-acid ligase from Bacillus subtilis

Acta Crystallogr F Struct Biol Commun. 2015 Sep;71(Pt 9):1125-30. doi: 10.1107/S2053230X15012698. Epub 2015 Aug 25.

Authors

Wataru Kagawa¹, Toshinobu Arai², Shun Ishikura², Kuniki Kino², Hitoshi Kurumizaka³

Affiliations

¹ Department of Interdisciplinary Science and Engineering, Program in Chemistry and Life Science, School of Science and Engineering, Meisei University, 2-1-1 Hodokubo, Hino-shi, Tokyo 191-8506, Japan.
² Department of Applied Chemistry, Faculty of Science and Engineering, Waseda University, 3-4-1 Ohkubo, Shinjuku-ku, Tokyo 169-8555, Japan.
³ Laboratory of Structural Biology, Graduate School of Advanced Science and Engineering, Waseda University, 2-2 Wakamatsu-cho, Shinjuku-ku, Tokyo 162-8480, Japan.

Abstract

RizA is an L-amino-acid ligase from Bacillus subtilis that participates in the biosynthesis of rhizocticin, an oligopeptide antibiotic. The substrate-free form of RizA has been crystallized and the structure was solved at 2.8 Å resolution. The amino-acid-binding site appears to be capable of accommodating multiple amino acids, consistent with previous biochemical studies.

Keywords: ATP-grasp fold; dipeptide synthesis; l-amino-acid ligase; rhizocticin.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Adenosine Triphosphate / metabolism
Amino Acids / metabolism*
Bacillus subtilis / enzymology*
Bacterial Proteins / chemistry*
Bacterial Proteins / metabolism
Binding Sites
Crystallography, X-Ray
Dipeptides / chemistry
Dipeptides / metabolism
Ligases / chemistry*
Ligases / metabolism
Models, Molecular
Protein Structure, Tertiary
Substrate Specificity

Substances

Amino Acids
Bacterial Proteins
Dipeptides
Adenosine Triphosphate
Ligases

Associated data

PDB/4WD3