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

Thumbnail Image

Files

High-resolution structure of the alcohol de­hydrogenase domain of the bifunctional bacterial enzyme AdhE.pdf (1.35 MB)

Date

2020

Authors

Journal Title

Journal ISSN

Volume Title

Publisher

John Wiley and Sons Ltd

Research Projects

Organizational Units

Journal Issue

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. Keywords: alcohol dehydrogenase; AdhE; Escherichia coli

Description

Volume 76| Part 9| September 2020| Pages 414-421

Keywords

alcohol dehydrogenase;, AdhE;, Escherichia coli, alcohol dehydrogenase domain of AdhE,, 6sci;, NAD-bound,, 6scg

Citation

URI

https://journals.iucr.org/f/issues/2020/09/00/no5171/index.html
 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7470043/
 https://oarep.usim.edu.my/handle/123456789/3944

Collections

Other Publications