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Aldehyde-alcohol dehydrogenase forms a high-order spirosome architecture critical for its activity

DOI: 10.1038/s41467-019-12427-8 DOI Help

Authors: Gijeong Kim (korea Advanced Institute of Science and Technology (KAIST)) , Liyana Azmi (University of Glasgow) , Seongmin Jang (Korea Advanced Institute of Science and Technology (KAIST)) , Taeyang Jung (Korea Advanced Institute of Science and Technology (KAIST); KTH Royal Institute of Technology; Karolinska Institutet) , Hans Hebert (KTH Royal Institute of Technology; Karolinska Institutet) , Andrew J. Roe (University of Glasgow) , Olwyn Byron (University of Glasgow) , Ji-Joon Song (Korea Advanced Institute of Science and Technology (KAIST))
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Communications , VOL 10

State: Published (Approved)
Published: October 2019
Diamond Proposal Number(s): 21440

Open Access Open Access

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.

Journal Keywords: Cryoelectron microscopy; Enzyme mechanisms

Diamond Keywords: Enzymes

Subject Areas: Biology and Bio-materials, Chemistry

Instruments: B21-High Throughput SAXS

Added On: 14/10/2019 14:10


Discipline Tags:

Biochemistry Chemistry Structural biology Life Sciences & Biotech

Technical Tags:

Scattering Small Angle X-ray Scattering (SAXS)