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

Authors :
Azmi L
Bragginton EC
Cadby IT
Byron O
Roe AJ
Lovering AL
Gabrielsen M
Source :
Acta crystallographica. Section F, Structural biology communications [Acta Crystallogr F Struct Biol Commun] 2020 Sep 01; Vol. 76 (Pt 9), pp. 414-421. Date of Electronic Publication: 2020 Aug 19.
Publication Year :
2020

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.<br /> (open access.)

Details

Language :
English
ISSN :
2053-230X
Volume :
76
Issue :
Pt 9
Database :
MEDLINE
Journal :
Acta crystallographica. Section F, Structural biology communications
Publication Type :
Academic Journal
Accession number :
32880589
Full Text :
https://doi.org/10.1107/S2053230X20010237