6AHC

Cryo-EM structure of aldehyde-alcohol dehydrogenase reveals a high-order helical architecture critical for its activity

Summary for 6AHC

• Entry DOI: 10.2210/pdb6ahc/pdb
• EMDB information: 9623
• Descriptor: Aldehyde-alcohol dehydrogenase (1 entity in total)
• Functional Keywords: acetyl coa, ethanol, regulation, high-order structure, hydrolase
• Biological source: Escherichia coli K-12
• Total number of polymer chains: 8
• Total formula weight: 771106.06

Authors

Kim, G.,Song, J.J. (deposition date: 2018-08-17, release date: 2019-08-21, Last modification date: 2024-03-27)

Primary citation

Kim, G.,Azmi, L.,Jang, S.,Jung, T.,Hebert, H.,Roe, A.J.,Byron, O.,Song, J.J.
Aldehyde-alcohol dehydrogenase forms a high-order spirosome architecture critical for its activity.
Nat Commun, 10:4527-4527, 2019

PubMed Abstract: Aldehyde-alcohol dehydrogenase (AdhE) is a key enzyme in bacterial fermentation, converting acetyl-CoA to ethanol, via two consecutive catalytic reactions. Here, we present a 3.5 Å resolution cryo-EM structure of full-length AdhE revealing a high-order spirosome architecture. The structure shows that the aldehyde dehydrogenase (ALDH) and alcohol dehydrogenase (ADH) active sites reside at the outer surface and the inner surface of the spirosome respectively, thus topologically separating these two activities. Furthermore, mutations disrupting the helical structure abrogate enzymatic activity, implying that formation of the spirosome structure is critical for AdhE activity. In addition, we show that this spirosome structure undergoes conformational change in the presence of cofactors. This work presents the atomic resolution structure of AdhE and suggests that the high-order helical structure regulates its enzymatic activity.

PubMed: 31586059
DOI: 10.1038/s41467-019-12427-8

Experimental method

ELECTRON MICROSCOPY (3.45 Å)