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

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 t...

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Autores principales: Azmi, Liyana, Bragginton, Eilis C., Cadby, Ian T., Byron, Olwyn, Roe, Andrew J., Lovering, Andrew L., Gabrielsen, Mads
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2020
Materias:
Research Communications
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7470043/
https://www.ncbi.nlm.nih.gov/pubmed/32880589
http://dx.doi.org/10.1107/S2053230X20010237
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author Azmi, Liyana
Bragginton, Eilis C.
Cadby, Ian T.
Byron, Olwyn
Roe, Andrew J.
Lovering, Andrew L.
Gabrielsen, Mads
author_facet Azmi, Liyana
Bragginton, Eilis C.
Cadby, Ian T.
Byron, Olwyn
Roe, Andrew J.
Lovering, Andrew L.
Gabrielsen, Mads
author_sort Azmi, Liyana
collection PubMed
description 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.
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spelling pubmed-74700432020-09-15 High-resolution structure of the alcohol dehydrogenase domain of the bifunctional bacterial enzyme AdhE Azmi, Liyana Bragginton, Eilis C. Cadby, Ian T. Byron, Olwyn Roe, Andrew J. Lovering, Andrew L. Gabrielsen, Mads Acta Crystallogr F Struct Biol Commun Research Communications 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. International Union of Crystallography 2020-08-19 /pmc/articles/PMC7470043/ /pubmed/32880589 http://dx.doi.org/10.1107/S2053230X20010237 Text en © Azmi et al. 2020 http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.http://creativecommons.org/licenses/by/4.0/
spellingShingle Research Communications
Azmi, Liyana
Bragginton, Eilis C.
Cadby, Ian T.
Byron, Olwyn
Roe, Andrew J.
Lovering, Andrew L.
Gabrielsen, Mads
High-resolution structure of the alcohol dehydrogenase domain of the bifunctional bacterial enzyme AdhE
title High-resolution structure of the alcohol dehydrogenase domain of the bifunctional bacterial enzyme AdhE
title_full High-resolution structure of the alcohol dehydrogenase domain of the bifunctional bacterial enzyme AdhE
title_fullStr High-resolution structure of the alcohol dehydrogenase domain of the bifunctional bacterial enzyme AdhE
title_full_unstemmed High-resolution structure of the alcohol dehydrogenase domain of the bifunctional bacterial enzyme AdhE
title_short High-resolution structure of the alcohol dehydrogenase domain of the bifunctional bacterial enzyme AdhE
title_sort high-resolution structure of the alcohol dehydrogenase domain of the bifunctional bacterial enzyme adhe
topic Research Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7470043/
https://www.ncbi.nlm.nih.gov/pubmed/32880589
http://dx.doi.org/10.1107/S2053230X20010237
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