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> | ||
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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 (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> | ||
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