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==Formate dehydrogenase - heterodisulfide reductase - formylmethanofuran dehydrogenase complex from Methanospirillum hungatei (heterodislfide reductase core and mobile arm in conformational state 1, composite structure)==
<StructureSection load='7bkd' size='340' side='right'caption='[[7bkd]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7bkd]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanospirillum_hungatei_JF-1 Methanospirillum hungatei JF-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BKD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BKD FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=9S8:2,4$l^{3},6$l^{3},8-tetrathia-1$l^{4},3$l^{2},5$l^{2},7$l^{2}-tetraferratricyclo[4.2.0.0^{1,4}]octane'>9S8</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</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=7bkd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bkd OCA], [https://pdbe.org/7bkd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bkd RCSB], [https://www.ebi.ac.uk/pdbsum/7bkd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bkd ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q2FKZ1_METHJ Q2FKZ1_METHJ] Part of a complex that catalyzes the reversible reduction of CoM-S-S-CoB to the thiol-coenzymes H-S-CoM (coenzyme M) and H-S-CoB (coenzyme B).[RuleBase:RU366072]
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== Publication Abstract from PubMed ==
The first reaction of the methanogenic pathway from carbon dioxide (CO(2)) is the reduction and condensation of CO(2) to formyl-methanofuran, catalyzed by formyl-methanofuran dehydrogenase (Fmd). Strongly reducing electrons for this reaction are generated by heterodisulfide reductase (Hdr) in complex with hydrogenase or formate dehydrogenase (Fdh) using a flavin-based electron-bifurcation mechanism. Here, we report enzymological and structural characterizations of Fdh-Hdr-Fmd complexes from Methanospirillum hungatei. The complexes catalyze this reaction using electrons from formate and the reduced form of the electron carrier F(420). Conformational changes in HdrA mediate electron bifurcation, and polyferredoxin FmdF directly transfers electrons to the CO(2) reduction site, as evidenced by methanofuran-dependent flavin-based electron bifurcation even without free ferredoxin, a diffusible electron carrier between Hdr and Fmd. Conservation of Hdr and Fmd structures suggests that this complex is common among hydrogenotrophic methanogens.

Three-megadalton complex of methanogenic electron-bifurcating and CO(2)-fixing enzymes.,Watanabe T, Pfeil-Gardiner O, Kahnt J, Koch J, Shima S, Murphy BJ Science. 2021 Sep 3;373(6559):1151-1156. doi: 10.1126/science.abg5550. Epub 2021 , Sep 1. PMID:34516836<ref>PMID:34516836</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 7bkd" style="background-color:#fffaf0;"></div>

==See Also==
*[[Formate dehydrogenase 3D structures|Formate dehydrogenase 3D structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Methanospirillum hungatei JF-1]]
[[Category: Murphy BJ]]
[[Category: Pfeil-Gardiner O]]
[[Category: Shima S]]
[[Category: Watanabe T]]