3ZDR

Structure of the Alcohol dehydrogenase (ADH) domain of a bifunctional ADHE dehydrogenase from Geobacillus thermoglucosidasius NCIMB 11955

3ZDR の概要

• エントリーDOI: 10.2210/pdb3zdr/pdb
• 分子名称: ALCOHOL DEHYDROGENASE DOMAIN OF THE BIFUNCTIONAL ACETALDEHYDE DEHYDROGENASE, ZINC ION, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: oxidoreductase, bifunctional alcohol/aldehyde dehydrogenase, bioethanol
• 由来する生物種: GEOBACILLUS THERMOGLUCOSIDASIUS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 48946.72

構造登録者

Extance, J.,Crennell, S.J.,Eley, K.,Cripps, R.,Hough, D.W.,Danson, M.J. (登録日: 2012-11-30, 公開日: 2013-10-02, 最終更新日: 2024-11-20)

主引用文献

Extance, J.,Crennell, S.J.,Eley, K.,Cripps, R.,Hough, D.W.,Danson, M.J.
Structure of a Bifunctional Alcohol Dehydrogenase Involved in Bioethanol Generation in Geobacillus Thermoglucosidasius
Acta Crystallogr.,Sect.D, 69:2104-, 2013

PubMed Abstract: Bifunctional alcohol/aldehyde dehydrogenase (ADHE) enzymes are found within many fermentative microorganisms. They catalyse the conversion of an acyl-coenzyme A to an alcohol via an aldehyde intermediate; this is coupled to the oxidation of two NADH molecules to maintain the NAD(+) pool during fermentative metabolism. The structure of the alcohol dehydrogenase (ADH) domain of an ADHE protein from the ethanol-producing thermophile Geobacillus thermoglucosidasius has been determined to 2.5 Å resolution. This is the first structure to be reported for such a domain. In silico modelling has been carried out to generate a homology model of the aldehyde dehydrogenase domain, and this was subsequently docked with the ADH-domain structure to model the structure of the complete ADHE protein. This model suggests, for the first time, a structural mechanism for the formation of the large multimeric assemblies or `spirosomes' that are observed for this ADHE protein and which have previously been reported for ADHEs from other organisms.

PubMed: 24100328
DOI: 10.1107/S0907444913020349

実験手法

X-RAY DIFFRACTION (2.504 Å)