4kpu | pdb_00004kpu

Electron transferring flavoprotein of Acidaminococcus fermentans: Towards a mechanism of flavin-based electron bifurcation

spinqualitylabelsall models 4kpu, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4kpu is a 2 chain structure with sequence from Acidaminococcus fermentans DSM 20731. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, FAD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function D2RIQ3_ACIFV Publication Abstract from PubMed Electron bifurcation is a fundamental strategy of energy coupling originally discovered in the Q-cycle of many organisms. Recently a flavin-based electron bifurcation has been detected in anaerobes, first in clostridia and later in acetogens and methanogens. It enables anaerobic bacteria and archaea to reduce the two [4Fe-4S] cluster-containing ferredoxin, an energy rich compound that is used to conduct difficult reductions as well as to increase the efficiency of substrate level and electron transport phosphorylations (SLP and ETP). Here we characterize the bifurcating electron transferring flavoprotein (EtfAf) and butyryl-CoA dehydrogenase (BcdAf) from Acidaminococcus fermentans which couple the exergonic reduction of crotonyl-CoA to butyryl-CoA to the endergonic reduction of ferredoxin both with NADH. EtfAf contains one FAD (alpha-FAD) in subunit alpha and a second FAD (beta-FAD) in subunit beta. The distance between the two isoalloxazine rings is 18 Angstrom. The EtfAf-NAD+ complex structure revealed beta-FAD as acceptor of the hydride of NADH. The formed beta-FADH- is considered as the bifurcating electron donor. Due to a conformational change, alpha-FAD is able to approach beta-FADH- by ca. 5 Angstrom and take up one electron yielding a stable anionic semiquinone, alpha-FAD-, which due to a second conformational change donates this electron further to FAD of BcdAf. The remaining non-stabilized neutral semiquinone, beta-FADH, immediately reduces ferredoxin. Repetition of this process affords a second reduced ferredoxin and FADH- of BcdAf that converts crotonyl-CoA to butyryl-CoA. Studies on the Mechanism of Electron Bifurcation Catalyzed by Electron Transferring Flavoprotein (Etf) and Butyryl-CoA Dehydrogenase (Bcd) of Acidaminococcus fermentans.,Palchowdhury N, Mowafy AM, Demmer JK, Upadhyay V, Koelzer S, Jayamani E, Kahnt J, Hornung M, Demmer U, Ermler U, Buckel W J Biol Chem. 2013 Dec 30. PMID:24379410 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA