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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4l2i]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Acidaminococcus_fermentans_DSM_20731 Acidaminococcus fermentans DSM 20731]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L2I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4L2I FirstGlance]. <br>
<table><tr><td colspan='2'>[[4l2i]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Acidaminococcus_fermentans_DSM_20731 Acidaminococcus fermentans DSM 20731]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L2I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4L2I FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.45&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</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=4l2i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l2i OCA], [https://pdbe.org/4l2i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4l2i RCSB], [https://www.ebi.ac.uk/pdbsum/4l2i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4l2i ProSAT]</span></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=4l2i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l2i OCA], [https://pdbe.org/4l2i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4l2i RCSB], [https://www.ebi.ac.uk/pdbsum/4l2i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4l2i ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/D2RIQ3_ACIFV D2RIQ3_ACIFV]  
[https://www.uniprot.org/uniprot/D2RIQ3_ACIFV D2RIQ3_ACIFV]  
<div style="background-color:#fffaf0;">
== 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<ref>PMID:24379410</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4l2i" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
</StructureSection>

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