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5ol2
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | The | + | ==The electron transferring flavoprotein/butyryl-CoA dehydrogenase complex from Clostridium difficile== |
| + | <StructureSection load='5ol2' size='340' side='right' caption='[[5ol2]], [[Resolution|resolution]] 3.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5ol2]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OL2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OL2 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=COS:COENZYME+A+PERSULFIDE'>COS</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ol2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ol2 OCA], [http://pdbe.org/5ol2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ol2 RCSB], [http://www.ebi.ac.uk/pdbsum/5ol2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ol2 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The electron transferring flavoprotein/butyryl-CoA dehydrogenase (EtfAB/Bcd) catalyzes the reduction of one crotonyl-CoA and two ferredoxins by two NADH within a flavin-based electron-bifurcating process. Here we report on the X-ray structure of the Clostridium difficile (EtfAB/Bcd)4 complex in the dehydrogenase-conducting D-state, alpha-FAD (bound to domain II of EtfA) and delta-FAD (bound to Bcd) being 8 A apart. Superimposing Acidaminococcus fermentans EtfAB onto C. difficile EtfAB/Bcd reveals a rotation of domain II of nearly 80 degrees . Further rotation by 10 degrees brings EtfAB into the bifurcating B-state, alpha-FAD and beta-FAD (bound to EtfB) being 14 A apart. This dual binding mode of domain II, substantiated by mutational studies, resembles findings in non-bifurcating EtfAB/acyl-CoA dehydrogenase complexes. In our proposed mechanism, NADH reduces beta-FAD, which bifurcates. One electron goes to ferredoxin and one to alpha-FAD, which swings over to reduce delta-FAD to the semiquinone. Repetition affords a second reduced ferredoxin and delta-FADH(-), which reduces crotonyl-CoA. | ||
| - | + | The semiquinone swing in the bifurcating electron transferring flavoprotein/butyryl-CoA dehydrogenase complex from Clostridium difficile.,Demmer JK, Pal Chowdhury N, Selmer T, Ermler U, Buckel W Nat Commun. 2017 Nov 17;8(1):1577. doi: 10.1038/s41467-017-01746-3. PMID:29146947<ref>PMID:29146947</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5ol2" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Buckel, W]] | ||
| + | [[Category: Chowdhury, N P]] | ||
| + | [[Category: Demmer, J K]] | ||
| + | [[Category: Ermler, U]] | ||
| + | [[Category: Selmer, T]] | ||
| + | [[Category: Acyl-coa dehydrogenase]] | ||
| + | [[Category: Bioenergetic]] | ||
| + | [[Category: Electron transferring flavoprotein]] | ||
| + | [[Category: Flavin based electron bifurcation]] | ||
| + | [[Category: Flavoprotein]] | ||
Revision as of 06:09, 29 November 2017
The electron transferring flavoprotein/butyryl-CoA dehydrogenase complex from Clostridium difficile
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