6KSY

Crystal structure of arginase from Zymomonas mobilis ZM4

6KSY の概要

• エントリーDOI: 10.2210/pdb6ksy/pdb
• 分子名称: Arginase/agmatinase/formiminoglutamase, ZINC ION (3 entities in total)
• 機能のキーワード: arginase, hydrolase
• 由来する生物種: Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 129142.23

構造登録者

Park, S.Y.,Hwangbo, S.A. (登録日: 2019-08-26, 公開日: 2020-08-05, 最終更新日: 2024-03-27)

主引用文献

Hwangbo, S.A.,Kim, J.W.,Jung, S.J.,Jin, K.S.,Lee, J.O.,Kim, J.S.,Park, S.Y.
Characterization of a Dimeric Arginase FromZymomonas mobilisZM4.
Front Microbiol, 10:2755-2755, 2019

PubMed Abstract: Many organisms have genes to protect themselves from toxic conditions such as high ethanol and/or ammonia concentrations. When a high ethanol condition is induced to ZM4, a representative ethanologenic organism, this bacterium overexpresses several genes to overcome this ethanol stress. Among them, we characterized a gene product annotated as an arginase (zmARG) from ZM4. Even though all of the arginase-determining sequence motifs are not strictly conserved in zmARG, this enzyme converts L-arginine to urea and L-ornithine in the presence of a divalent manganese ion. The revealed high-resolution crystal structure of zmARG shows that it has a typical globular α/β arginase fold with a protruded C-terminal helix. Two zinc ions reside in the active site, where one metal ion is penta-coordinated and the other has six ligands, discerning this zmARG from the reported arginases with two hexa-liganded metal ions. zmARG forms a dimeric structure in solution as well as in the crystalline state. The dimeric assembly of zmARG is formed mainly by interaction formed between the C-terminal α-helix of one molecule and the α/β hydrolase fold of another molecule. The presented findings demonstrate the first reported dimeric arginase formed by the C-terminal tail and has two metal ions coordinated by different number of ligands.

PubMed: 32038508
DOI: 10.3389/fmicb.2019.02755

実験手法

X-RAY DIFFRACTION (1.649 Å)