PDBsum entry 4mts

Lyase

PDB id: 4mts

Contents

Protein chains

129 a.a.

Ligands

GOL ×3

Metals

_NI

_ZN ×2

Waters ×266

PDB id:

4mts

Name:

Lyase

Title:

Ni- and zn-bound gloa2 at high resolution

Structure:

Lactoylglutathione lyase. Chain: a, b. Synonym: gloa2. Engineered: yes

Source:

Pseudomonas aeruginosa. Organism_taxid: 208964. Strain: atcc 15692 / pao1 / 1c / prs 101 / lmg 12228. Gene: gloa2, pa0710. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

1.80Å R-factor: 0.166 R-free: 0.201

Authors:

R.Bythell-Douglas,C.S.Bond

Key ref:

R.Bythell-Douglas et al. (2015). The crystal structure of a homodimeric Pseudomonas glyoxalase I enzyme reveals asymmetric metallation commensurate with half-of-sites activity. Chemistry, 21, 541-544. PubMed id: 25411134 DOI: 10.1002/chem.201405402

Date:

20-Sep-13 Release date: 24-Sep-14

Protein chains

Q9I5L8  (Q9I5L8_PSEAE) -  Aldoketomutase from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)

Seq: 131 a.a.

Struc: 129 a.a.

Enzyme reactions

• Enzyme class: E.C.4.4.1.5 - lactoylglutathione lyase.
• Reaction: (R)-S-lactoylglutathione = methylglyoxal + glutathione

(R)-S-lactoylglutathione = methylglyoxal + glutathione (Bound ligand (Het Group name = GOL) matches with 83.33% similarity)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1002/chem.201405402

Chemistry 21:541-544 (2015)

PubMed id: 25411134

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

R.Bythell-Douglas, U.Suttisansanee, G.R.Flematti, M.Challenor, M.Lee, S.Panjikar, J.F.Honek, C.S.Bond.

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.