6FAH

Molecular basis of the flavin-based electron-bifurcating caffeyl-CoA reductase reaction

Summary for 6FAH

• Entry DOI: 10.2210/pdb6fah/pdb
• Descriptor: Caffeyl-CoA reductase-Etf complex subunit CarE, Caffeyl-CoA reductase-Etf complex subunit CarD, Caffeyl-CoA reductase-Etf complex subunit CarC, ... (6 entities in total)
• Functional Keywords: acetogenic bacteria, bioenergetics, flavin-based electron bifurcation, electron-transfer protein/acyl-coa dehydrogenase, ferredoxin, flavoprotein
• Biological source: Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1); More
• Cellular location: Cytoplasm : H6LGM8 H6LGM7 H6LGM6
• Total number of polymer chains: 6
• Total formula weight: 231360.91

Authors

Demmer, J.K.,Bertsch, J.,Oeppinger, C.,Wohlers, H.,Kayastha, K.,Demmer, U.,Ermler, U.,Mueller, V. (deposition date: 2017-12-15, release date: 2018-01-24, Last modification date: 2025-10-01)

Primary citation

Demmer, J.K.,Bertsch, J.,Oppinger, C.,Wohlers, H.,Kayastha, K.,Demmer, U.,Ermler, U.,Muller, V.
Molecular basis of the flavin-based electron-bifurcating caffeyl-CoA reductase reaction.
FEBS Lett., 592:332-342, 2018

PubMed Abstract: Flavin-based electron bifurcation (FBEB) is a recently discovered mode of energy coupling in anaerobic microorganisms. The electron-bifurcating caffeyl-CoA reductase (CarCDE) catalyzes the reduction of caffeyl-CoA and ferredoxin by oxidizing NADH. The 3.5 Å structure of the heterododecameric Car(CDE) complex of Acetobacterium woodii, presented here, reveals compared to other electron-transferring flavoprotein/acyl dehydrogenase family members an additional ferredoxin-like domain with two [4Fe-4S] clusters N-terminally fused to CarE. It might serve, in vivo, as specific adaptor for the physiological electron acceptor. Kinetic analysis of a CarCDE(∆Fd) complex indicates the bypassing of the ferredoxin-like domain by artificial electron acceptors. Site-directed mutagenesis studies substantiated the crucial role of the C-terminal arm of CarD and of ArgE203, hydrogen-bonded to the bifurcating FAD, for FBEB.

PubMed: 29325219
DOI: 10.1002/1873-3468.12971

Experimental method

X-RAY DIFFRACTION (3.133 Å)