3BFJ

Crystal structure analysis of 1,3-propanediol oxidoreductase

3BFJ の概要

• エントリーDOI: 10.2210/pdb3bfj/pdb
• 分子名称: 1,3-propanediol oxidoreductase, FE (II) ION (3 entities in total)
• 機能のキーワード: opportunistic pathogens, decamer, structural genomics, structural proteomics in europe, spine, oxidoreductase
• 由来する生物種: Klebsiella pneumoniae
• タンパク質・核酸の鎖数: 20
• 化学式量合計: 832888.46

構造登録者

Marcal, D.,Enguita, F.J.,Carrondo, M.A.,Structural Proteomics in Europe (SPINE) (登録日: 2007-11-21, 公開日: 2008-11-25, 最終更新日: 2024-02-21)

主引用文献

Marcal, D.,Rego, A.T.,Carrondo, M.A.,Enguita, F.J.
1,3-propanediol dehydrogenase from Klebsiella pneumoniae: decameric quaternary structure and possible subunit cooperativity
J.Bacteriol., 191:1143-1151, 2009

PubMed Abstract: Klebsiella pneumoniae is a nosocomial pathogen frequently isolated from opportunistic infections, especially in clinical environments. In spite of its potential pathogenicity, this microorganism has several metabolic potentials that could be used in biotechnology applications. K. pneumoniae is able to metabolize glycerol as a sole source of carbon and energy. 1,3-Propanediol dehydrogenase is the core of the metabolic pathway for the use of glycerol. We have determined the crystallographic structure of 1,3-propanediol dehydrogenase, a type III Fe-NAD-dependent alcohol dehydrogenase, at 2.7-A resolution. The structure of the enzyme monomer is closely related to that of other alcohol dehydrogenases. The overall arrangement of the enzyme showed a decameric structure, formed by a pentamer of dimers, which is the catalytic form of the enzyme. Dimers are associated by strong ionic interactions that are responsible for the highly stable in vivo packing of the enzyme. Kinetic properties of the enzyme as determined in the article would suggest that this decameric arrangement is related to the cooperativity between monomers.

PubMed: 19011020
DOI: 10.1128/JB.01077-08

実験手法

X-RAY DIFFRACTION (2.7 Å)