5ol2 | pdb_00005ol2

The electron transferring flavoprotein/butyryl-CoA dehydrogenase complex from Clostridium difficile

spinqualitylabelsall models 5ol2, resolution 3.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ol2 is a 6 chain structure with sequence from Clostridioides difficile. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.1Å Ligands: CA, COS, FAD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A125V455_9CAUD 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Acyl-CoA dehydrogenase 3D structures

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