High-resolution structure of the alcohol dehydrogenase domain of the bifunctional bacterial enzyme AdhE

DOI: 10.1107/S2053230X20010237

Authors: Liyana Azmi (University of Glasgow) , Eilis C. Bragginton (University of Birmingham) , Ian T. Cadby (University of Birmingham) , Olwyn Byron (University of Glasgow) , Andrew Roe (University of Glasgow) , Andrew L. Lovering (University of Birmingham) , Mads Gabrielsen (CRUK Beatson Institute)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section F Structural Biology Communications , VOL 76 , PAGES 414 - 421

State: Published (Approved)
Published: September 2020
Diamond Proposal Number(s): 12112 , 11651

Abstract: The bifunctional alcohol/aldehyde dehydrogenase (AdhE) comprises both an N-terminal aldehyde dehydrogenase (AldDH) and a C-terminal alcohol dehydrogenase (ADH). In vivo, full-length AdhE oligomerizes into long oligomers known as spirosomes. However, structural analysis of AdhE is challenging owing to the heterogeneity of the spirosomes. Therefore, the domains of AdhE are best characterized separately. Here, the structure of ADH from the pathogenic Escherichia coli O157:H7 was determined to 1.65 Å resolution. The dimeric crystal structure was confirmed in solution by small-angle X-ray scattering.

Journal Keywords: alcohol dehydrogenase; AdhE; Escherichia coli

Diamond Keywords: Bacteria; Enzymes

Subject Areas: Biology and Bio-materials


Instruments: I03-Macromolecular Crystallography , I04-1-Macromolecular Crystallography (fixed wavelength)

Added On: 09/09/2020 10:29

Documents:
no5171.pdf

Discipline Tags:

Pathogens Health & Wellbeing Structural biology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)