6SCI

Structure of AdhE form 1

Summary for 6SCI

• Entry DOI: 10.2210/pdb6sci/pdb
• Related: 6SCG
• Descriptor: Aldehyde-alcohol dehydrogenase, FE (III) ION (3 entities in total)
• Functional Keywords: aldehyde alcohol dehydrogenase, oxidoreductase
• Biological source: Escherichia coli (strain K12)
• Total number of polymer chains: 2
• Total formula weight: 99901.79

Authors

Lovering, A.L.,Bragginton, E. (deposition date: 2019-07-24, release date: 2020-08-26, Last modification date: 2024-01-24)

Primary citation

Azmi, L.,Bragginton, E.C.,Cadby, I.T.,Byron, O.,Roe, A.J.,Lovering, A.L.,Gabrielsen, M.
High-resolution structure of the alcohol dehydrogenase domain of the bifunctional bacterial enzyme AdhE.
Acta Crystallogr.,Sect.F, 76:414-421, 2020

PubMed 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.

PubMed: 32880589
DOI: 10.1107/S2053230X20010237

Experimental method

X-RAY DIFFRACTION (1.95 Å)