PDBsum entry 4pvc

Oxidoreductase

PDB id: 4pvc

Contents

Protein chains

342 a.a.

Waters ×346

PDB id:

4pvc

Name:

Oxidoreductase

Title:

Crystal structure of yeast methylglyoxal/ isovaleraldehyde reductase gre2

Structure:

NADPH-dependent methylglyoxal reductase gre2. Chain: a, b. Synonym: 3-methylbutanal reductase, genes de respuesta a estres protein 2, isovaleraldehyde reductase. Engineered: yes

Source:

Saccharomyces cerevisiae. Yeast. Organism_taxid: 559292. Strain: s288c. Gene: gre2, yol151w. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.00Å R-factor: 0.226 R-free: 0.266

Authors:

P.C.Guo,Z.Z.Bao,W.F.Li,C.Z.Zhou

Key ref:

P.C.Guo et al. (2014). Structural insights into the cofactor-assisted substrate recognition of yeast methylglyoxal/isovaleraldehyde reductase Gre2. Biochim Biophys Acta, 1844, 1486-1492. PubMed id: 24879127 DOI: 10.1016/j.bbapap.2014.05.008

Date:

17-Mar-14 Release date: 22-Oct-14

Protein chains

Q12068  (GRE2_YEAST) -  NADPH-dependent methylglyoxal reductase GRE2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 342 a.a.

Struc: 342 a.a.

Enzyme reactions

• Enzyme class 1: E.C.1.1.1.265 - 3-methylbutanal reductase.
• Reaction:
  1. 3-methylbutanol + NADP⁺ = 3-methylbutanal + NADPH + H⁺
  2. 3-methylbutanol + NAD⁺ = 3-methylbutanal + NADH + H⁺
• Enzyme class 2: E.C.1.1.1.283 - methylglyoxal reductase (NADPH).
• Reaction: (S)-lactaldehyde + NADP⁺ = methylglyoxal + NADPH + H⁺

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

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

reference

DOI no: 10.1016/j.bbapap.2014.05.008

Biochim Biophys Acta 1844:1486-1492 (2014)

PubMed id: 24879127

Structural insights into the cofactor-assisted substrate recognition of yeast methylglyoxal/isovaleraldehyde reductase Gre2.

P.C.Guo, Z.Z.Bao, X.X.Ma, Q.Xia, W.F.Li.

ABSTRACT

Saccharomyces cerevisiae Gre2 (EC1.1.1.283) serves as a versatile enzyme that catalyzes the stereoselective reduction of a broad range of substrates including aliphatic and aromatic ketones, diketones, as well as aldehydes, using NADPH as the cofactor. Here we present the crystal structures of Gre2 from S. cerevisiae in an apo-form at 2.00Å and NADPH-complexed form at 2.40Å resolution. Gre2 forms a homodimer, each subunit of which contains an N-terminal Rossmann-fold domain and a variable C-terminal domain, which participates in substrate recognition. The induced fit upon binding to the cofactor NADPH makes the two domains shift toward each other, producing an interdomain cleft that better fits the substrate. Computational simulation combined with site-directed mutagenesis and enzymatic activity analysis enabled us to define a potential substrate-binding pocket that determines the stringent substrate stereoselectivity for catalysis.