Structure of a bifunctional alcohol dehydrogenase involved in bioethanol generation in Geobacillus thermoglucosidasius

Jonathan Extance, Susan J. Crennell, Kirstin Eley, Roger Cripps, David W. Hough, Michael J. Danson

Research output: Contribution to journalArticle

18 Citations (Scopus)
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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 2.514;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.
Original languageEnglish
Pages (from-to)2104-2115
Number of pages12
JournalActa Crystallographica Section D-Biological Crystallography
Volume69
Issue number10
DOIs
Publication statusPublished - Oct 2013

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