7bkb
From Proteopedia
(Difference between revisions)
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| - | ==== | + | ==Formate dehydrogenase - heterodisulfide reductase - formylmethanofuran dehydrogenase complex from Methanospirillum hungatei (hexameric, composite structure)== |
| - | <StructureSection load='7bkb' size='340' side='right'caption='[[7bkb]]' scene=''> | + | <StructureSection load='7bkb' size='340' side='right'caption='[[7bkb]], [[Resolution|resolution]] 3.50Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7bkb]] is a 20 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=7BKB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BKB FirstGlance]. <br> |
| - | </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=7bkb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bkb OCA], [https://pdbe.org/7bkb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bkb RCSB], [https://www.ebi.ac.uk/pdbsum/7bkb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bkb ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.5Å</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>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=MGD:2-AMINO-5,6-DIMERCAPTO-7-METHYL-3,7,8A,9-TETRAHYDRO-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-4-ONE+GUANOSINE+DINUCLEOTIDE'>MGD</scene>, <scene name='pdbligand=MO:MOLYBDENUM+ATOM'>MO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=7bkb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bkb OCA], [https://pdbe.org/7bkb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bkb RCSB], [https://www.ebi.ac.uk/pdbsum/7bkb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bkb ProSAT]</span></td></tr> | ||
</table> | </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] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7bkb" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Formate dehydrogenase 3D structures|Formate dehydrogenase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Methanospirillum hungatei JF-1]] |
| + | [[Category: Murphy BJ]] | ||
| + | [[Category: Pfeil-Gardiner O]] | ||
| + | [[Category: Shima S]] | ||
| + | [[Category: Watanabe T]] | ||
Current revision
Formate dehydrogenase - heterodisulfide reductase - formylmethanofuran dehydrogenase complex from Methanospirillum hungatei (hexameric, composite structure)
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