Journal:Acta Cryst F:S2053230X20010237
From Proteopedia
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<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. | ||
<b>References</b><br> | <b>References</b><br> | ||
Revision as of 12:28, 1 September 2020
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