6tqm
From Proteopedia
(Difference between revisions)
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| - | == | + | ==Escherichia coli AdhE structure in its compact conformation== |
| - | <StructureSection load='6tqm' size='340' side='right'caption='[[6tqm]]' scene=''> | + | <StructureSection load='6tqm' size='340' side='right'caption='[[6tqm]], [[Resolution|resolution]] 3.80Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TQM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TQM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6tqm]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TQM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TQM FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6tqm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tqm OCA], [https://pdbe.org/6tqm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tqm RCSB], [https://www.ebi.ac.uk/pdbsum/6tqm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tqm ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.8Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=TXE:[[(2R,3S,4R,5R)-5-[(3R)-3-aminocarbonyl-3,4-dihydro-2H-pyridin-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanidyl-ph+osphoryl]+[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl+phosphate'>TXE</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6tqm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tqm OCA], [https://pdbe.org/6tqm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tqm RCSB], [https://www.ebi.ac.uk/pdbsum/6tqm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tqm ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ADHE_ECOLI ADHE_ECOLI] This enzyme has three activities: ADH, ACDH, and PFL-deactivase. In aerobic conditions it acts as a hydrogen peroxide scavenger. The PFL deactivase activity catalyzes the quenching of the pyruvate-formate-lyase catalyst in an iron, NAD, and CoA dependent reaction. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Acetaldehyde-alcohol dehydrogenase (AdhE) enzymes are a key metabolic enzyme in bacterial physiology and pathogenicity. They convert acetyl-CoA to ethanol via an acetaldehyde intermediate during ethanol fermentation in an anaerobic environment. This two-step reaction is associated to NAD(+) regeneration, essential for glycolysis. The bifunctional AdhE enzyme is conserved in all bacterial kingdoms but also in more phylogenetically distant microorganisms such as green microalgae. It is found as an oligomeric form called spirosomes, for which the function remains elusive. Here, we use cryo-electron microscopy to obtain structures of Escherichia coli spirosomes in different conformational states. We show that spirosomes contain active AdhE monomers, and that AdhE filamentation is essential for its activity in vitro and function in vivo. The detailed analysis of these structures provides insight showing that AdhE filamentation is essential for substrate channeling within the filament and for the regulation of enzyme activity. | ||
| + | |||
| + | Filamentation of the bacterial bi-functional alcohol/aldehyde dehydrogenase AdhE is essential for substrate channeling and enzymatic regulation.,Pony P, Rapisarda C, Terradot L, Marza E, Fronzes R Nat Commun. 2020 Mar 18;11(1):1426. doi: 10.1038/s41467-020-15214-y. PMID:32188856<ref>PMID:32188856</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6tqm" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Escherichia coli K-12]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Fronzes R]] |
| + | [[Category: Pony P]] | ||
Current revision
Escherichia coli AdhE structure in its compact conformation
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