Journal:Acta Cryst F:S2053230X20010237
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| - | <StructureSection load='' size='450' side='right' scene=' | + | <StructureSection load='' size='450' side='right' scene='85/859650/Cv/2' caption=''> |
===High-resolution structure of alcohol dehydrogenase from the bifunctional bacterial enzyme AdhE=== | ===High-resolution structure of alcohol dehydrogenase from the bifunctional bacterial enzyme AdhE=== | ||
<big>Liyana Azmi, Eilis C. Bragginton, Ian T. Cadby, Olwyn Byron, Andrew J. Roe, Andrew L. Lovering and Mads Gabrielsen</big> <ref>doi 10.1107/S2053230X20010237</ref> | <big>Liyana Azmi, Eilis C. Bragginton, Ian T. Cadby, Olwyn Byron, Andrew J. Roe, Andrew L. Lovering and Mads Gabrielsen</big> <ref>doi 10.1107/S2053230X20010237</ref> | ||
<hr/> | <hr/> | ||
<b>Molecular Tour</b><br> | <b>Molecular Tour</b><br> | ||
| + | The bifunctional aldehyde/alcohol dehydrogenase (AdhE) is a protein of many uses. Genomic studies showed that AdhE is a viable target for anti-virulence compounds. On the other hand, residual mutations of AdhE led to the increased production of ethanol for biofuel generation. Thus, structural information of AdhE is crucial for the genetic modification of the protein to enhance biofuel production and allow structure-based drug design for anti-virulence therapies. | ||
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| + | AdhE is an interesting protein by the virtue of its structural assembly. Multiple copies of AdhE self-oligomerises to form spiral protomers known as spirosomes. However, the heterogeneity of these spirosomes make structural characterisation complex thus, separation of the domains allows more structural and biochemical depiction of AdhE. | ||
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| + | Here, we have individually characterised the structure of the N-terminal, alcohol dehydrogenase (ADH). ADH crystallised with a homodimer formation, which is also adopted in the spirosome assembly in AdhE. Interestingly, this conformation is also highly conserved with other alcohol dehydrogenases in other species. Comparison to the high-resolution structure of AdhE showed that a missing loop in ADH is stabilised by the C-terminal aldehyde dehydrogenase and shows the importance of the interaction for the functionality of AdhE as a whole. | ||
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| + | <scene name='85/859650/Cv/3'>Cartoon representation of a monomer of the ADH domain of AdhE from E. coli.</scene>. The two subdomains are coloured slate (N-terminal) and teal (C-terminal), with NAD represented by green sticks and Fe2+ ions by orange spheres (PDB entry [[6scg]]). | ||
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| + | <scene name='85/859650/Cv/4'>Cartoon representation of the oligomeric assembly</scene>, in which the two subunits forming the dimer are coloured separately. | ||
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| + | <scene name='85/859650/Cv/6'>Crystal structure of ADH superposed on the full-length spirosome of AdhE</scene> (PDB entry [[6ahc]]). | ||
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| + | <scene name='85/859650/Cv/11'>Close-up of the pocket where NAD is bound to the ADH structure</scene>. Water molecules are shown as red spheres. | ||
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| + | '''PDB references:''' alcohol dehydrogenase domain of AdhE, [[6sci]]; NAD-bound, [[6scg]] | ||
<b>References</b><br> | <b>References</b><br> | ||
Current revision
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