4MTR

Zn-bound GloA2

4MTR の概要

• エントリーDOI: 10.2210/pdb4mtr/pdb
• 関連するPDBエントリー: 4MTQ 4MTS 4MTT
• 分子名称: Lactoylglutathione lyase, 1,2-ETHANEDIOL, ZINC ION, ... (4 entities in total)
• 機能のキーワード: isomerase, hydrolase, metal binding, lyase
• 由来する生物種: Pseudomonas aeruginosa
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 30272.81

構造登録者

Bythell-Douglas, R.,Bond, C.S. (登録日: 2013-09-20, 公開日: 2014-09-24, 最終更新日: 2023-09-20)

主引用文献

Bythell-Douglas, R.,Suttisansanee, U.,Flematti, G.R.,Challenor, M.,Lee, M.,Panjikar, S.,Honek, J.F.,Bond, C.S.
The crystal structure of a homodimeric Pseudomonas glyoxalase I enzyme reveals asymmetric metallation commensurate with half-of-sites activity.
Chemistry, 21:541-544, 2015

PubMed Abstract: The Zn inactive class of glyoxalase I (Glo1) metalloenzymes are typically homodimeric with two metal-dependent active sites. While the two active sites share identical amino acid composition, this class of enzyme is optimally active with only one metal per homodimer. We have determined the X-ray crystal structure of GloA2, a Zn inactive Glo1 enzyme from Pseudomonas aeruginosa. The presented structures exhibit an unprecedented metal-binding arrangement consistent with half-of-sites activity: one active site contains a single activating Ni(2+) ion, whereas the other contains two inactivating Zn(2+) ions. Enzymological experiments prompted by the binuclear Zn(2+) site identified a novel catalytic property of GloA2. The enzyme can function as a Zn(2+) /Co(2+) -dependent hydrolase, in addition to its previously determined glyoxalase I activity. The presented findings demonstrate that GloA2 can accommodate two distinct metal-binding arrangements simultaneously, each of which catalyzes a different reaction.

PubMed: 25411134
DOI: 10.1002/chem.201405402

実験手法

X-RAY DIFFRACTION (1.83 Å)