Liyana Azmi
@usim.edu.my
Faculty of Medicine an Health Sciences
Universiti Sains Islam Malaysia
RESEARCH INTERESTS
Microbiology, Structural biology
Scopus Publications
Scholar Citations
Scholar h-index
Scholar i10-index
Scopus Publications
Liyana Azmi, Eilis C. Bragginton, Ian T. Cadby, Olwyn Byron, Andrew J. Roe, Andrew L. Lovering, and Mads Gabrielsen
International Union of Crystallography (IUCr)
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.
Gijeong Kim, Liyana Azmi, Seongmin Jang, Taeyang Jung, Hans Hebert, Andrew J. Roe, Olwyn Byron, and Ji-Joon Song
Springer Science and Business Media LLC
AbstractAldehyde-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.
Michaela J. Conley, Marion McElwee, Liyana Azmi, Mads Gabrielsen, Olwyn Byron, Ian G. Goodfellow, and David Bhella
Springer Science and Business Media LLC