PDBsum entry 3b3d

Oxidoreductase

PDB id: 3b3d

Contents

Protein chains

280 a.a. *

Metals

_CA ×4

Waters ×256

* Residue conservation analysis

PDB id:

3b3d

Name:

Oxidoreductase

Title:

B.Subtilis ytbe

Structure:

Putative morphine dehydrogenase. Chain: a, b, c. Synonym: ytbe protein. Engineered: yes

Source:

Bacillus subtilis. Organism_taxid: 1423. Gene: ytbe. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.30Å R-factor: 0.196 R-free: 0.260

Authors:

Y.F.Zhou,L.F.Li,Y.H.Liang,X.-D.Su

Key ref:

J.Lei et al. (2009). Structural and biochemical analyses of YvgN and YtbE from Bacillus subtilis. Protein Sci, 18, 1792-1800. PubMed id: 19585557

Date:

20-Oct-07 Release date: 21-Oct-08

Protein chains

O34678  (YTBE_BACSU) -  Uncharacterized oxidoreductase YtbE from Bacillus subtilis (strain 168)

Seq: 280 a.a.

Struc: 280 a.a.

Enzyme reactions

• Enzyme class: E.C.1.-.-.-

Protein Sci 18:1792-1800 (2009)

PubMed id: 19585557

Structural and biochemical analyses of YvgN and YtbE from Bacillus subtilis.

J.Lei, Y.F.Zhou, L.F.Li, X.D.Su.

ABSTRACT

Bacillus subtilis is one of the most studied gram-positive bacteria. In this work, YvgN and YtbE from B. subtilis, assigned as AKR5G1 and AKR5G2 of aldo-keto reductase (AKR) superfamily. AKR catalyzes the NADPH-dependent reduction of aldehyde or aldose substrates to alcohols. YvgN and YtbE were studied by crystallographic and enzymatic analyses. The apo structures of these proteins were determined by molecular replacement, and the structure of holoenzyme YvgN with NADPH was also solved, revealing the conformational changes upon cofactor binding. Our biochemical data suggest both YvgN and YtbE have preferential specificity for derivatives of benzaldehyde, such as nitryl or halogen group substitution at the 2 or 4 positions. These proteins also showed broad catalytic activity on many standard substrates of AKR, such as glyoxal, dihydroxyacetone, and DL-glyceraldehyde, suggesting a possible role in bacterial detoxification.