The crystal structure of a homodimeric Pseudomonas glyoxalase I enzyme reveals asymmetric metallation commensurate with half-of-sites activity

Rohan Bythell-Douglas, Uthaiwan Suttisansanee, Gavin R. Flematti, Michael Challenor, Mihwa Lee, Santosh Panjikar, John F. Honek, Charles S. Bond

Research output: Contribution to journalArticlepeer-review

13 Citations (Scopus)

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 Ni2+ ion, whereas the other contains two inactivating Zn2+ ions. Enzymological experiments prompted by the binuclear Zn2+ site identified a novel catalytic property of GloA2. The enzyme can function as a Zn2+/Co2+ -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.

Original languageEnglish
Pages (from-to)541-544
Number of pages4
JournalChemistry - A European Journal
Volume21
Issue number2
DOIs
Publication statusPublished - 7 Jan 2015

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