Journal:Acta Cryst F:S2053230X20010237
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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. | 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. | ||
<b>References</b><br> | <b>References</b><br> | ||
Revision as of 13:23, 1 September 2020
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