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

Wataru Kagawa^*, Toshinobu Arai, Shun Ishikura, Kuniki Kino, Hitoshi Kurumizaka

^*Corresponding author for this work

School of Advanced Science and Engineering

Research output: Contribution to journal › Article › peer-review

9 Citations (Scopus)

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.

Original language	English
Pages (from-to)	1125-1130
Number of pages	6
Journal	Acta Crystallographica Section:F Structural Biology Communications
Volume	71
DOIs	https://doi.org/10.1107/S2053230X15012698
Publication status	Published - 2015 Sept 1

Keywords

ATP-grasp fold
dipeptide synthesis
l-amino-acid ligase
rhizocticin

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Genetics
Condensed Matter Physics

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10.1107/S2053230X15012698

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title = "Structure of RizA, an l-amino-acid ligase from Bacillus subtilis",

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 {\AA} 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",

author = "Wataru Kagawa and Toshinobu Arai and Shun Ishikura and Kuniki Kino and Hitoshi Kurumizaka",

note = "Publisher Copyright: {\textcopyright} 2015 International Union of Crystallography.",

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doi = "10.1107/S2053230X15012698",

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T1 - Structure of RizA, an l-amino-acid ligase from Bacillus subtilis

AU - Kagawa, Wataru

AU - Arai, Toshinobu

AU - Ishikura, Shun

AU - Kino, Kuniki

AU - Kurumizaka, Hitoshi

PY - 2015/9/1

Y1 - 2015/9/1

N2 - 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.

AB - 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.

KW - ATP-grasp fold

KW - dipeptide synthesis

KW - l-amino-acid ligase

KW - rhizocticin

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JO - Acta Crystallographica Section:F Structural Biology Communications

JF - Acta Crystallographica Section:F Structural Biology Communications

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

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