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4l1f

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Revision as of 09:26, 7 December 2022

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

Structural highlights

4l1f 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:	, , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

D2RL84_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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Palchowdhury N, Mowafy AM, Demmer JK, Upadhyay V, Koelzer S, Jayamani E, Kahnt J, Hornung M, Demmer U, Ermler U, Buckel W. Studies on the Mechanism of Electron Bifurcation Catalyzed by Electron Transferring Flavoprotein (Etf) and Butyryl-CoA Dehydrogenase (Bcd) of Acidaminococcus fermentans. J Biol Chem. 2013 Dec 30. PMID:24379410 doi:http://dx.doi.org/10.1074/jbc.M113.521013

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4l1f"

@@ Line 3: / Line 3: @@
 <StructureSection load='4l1f' size='340' side='right'caption='[[4l1f]], [[Resolution|resolution]] 1.79&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4l1f]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Acidaminococcus_fermentans Acidaminococcus fermentans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L1F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4L1F FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4l1f]] 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=4L1F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4L1F FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COS:COENZYME+A+PERSULFIDE'>COS</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PDO:1,3-PROPANDIOL'>PDO</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COS:COENZYME+A+PERSULFIDE'>COS</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PDO:1,3-PROPANDIOL'>PDO</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4kpu|4kpu]], [[4l2i|4l2i]]</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=4l1f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l1f OCA], [https://pdbe.org/4l1f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4l1f RCSB], [https://www.ebi.ac.uk/pdbsum/4l1f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4l1f ProSAT]</span></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=4l1f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l1f OCA], [http://pdbe.org/4l1f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4l1f RCSB], [http://www.ebi.ac.uk/pdbsum/4l1f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4l1f ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/D2RL84_ACIFV D2RL84_ACIFV]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 21: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Acidaminococcus fermentans]]
+[[Category: Acidaminococcus fermentans DSM 20731]]
 [[Category: Large Structures]]
-[[Category: Buckel, W]]
+[[Category: Buckel W]]
-[[Category: Chowdhury, N P]]
+[[Category: Chowdhury NP]]
-[[Category: Demmer, J]]
+[[Category: Demmer J]]
-[[Category: Demmer, U]]
+[[Category: Demmer U]]
-[[Category: Ermler, U]]
+[[Category: Ermler U]]
-[[Category: Jayamani, E]]
+[[Category: Jayamani E]]
-[[Category: Kahnt, J]]
+[[Category: Kahnt J]]
-[[Category: Kolzer, S]]
+[[Category: Kolzer S]]
-[[Category: Mowafy, A M]]
+[[Category: Mowafy AM]]
-[[Category: Upadhyay, V]]
+[[Category: Upadhyay V]]
-[[Category: Butyryl-coa dehydrogenase]]
-[[Category: Electron transport]]
-[[Category: Fad]]
-[[Category: Nadh]]

4l1f

From Proteopedia

Revision as of 09:26, 7 December 2022

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

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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