4MTS

Ni- and Zn-bound GloA2 at high resolution

Summary for 4MTS

• Entry DOI: 10.2210/pdb4mts/pdb
• Related: 4MTQ 4MTR 4MTT
• Descriptor: Lactoylglutathione lyase, GLYCEROL, NICKEL (II) ION, ... (5 entities in total)
• Functional Keywords: isomerase, hydrolase, metal binding, lyase
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 2
• Total formula weight: 30359.51

Authors

Bythell-Douglas, R.,Bond, C.S. (deposition date: 2013-09-20, release date: 2014-09-24, Last modification date: 2023-09-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.8 Å)