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{{Large structure}}
 
==TUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE FROM METHANOTHERMOBACTER WOLFEII, TRICLINIC FORM AT 2.55 A==
==TUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE FROM METHANOTHERMOBACTER WOLFEII, TRICLINIC FORM AT 2.55 A==
<StructureSection load='5t61' size='340' side='right' caption='[[5t61]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
<StructureSection load='5t61' size='340' side='right'caption='[[5t61]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5t61]] is a 48 chain structure with sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_sp._cat2 Methanothermobacter sp. cat2] and [http://en.wikipedia.org/wiki/Methanothermobacter_wolfeii Methanothermobacter wolfeii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T61 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5T61 FirstGlance]. <br>
<table><tr><td colspan='2'>[[5t61]] is a 48 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanothermobacter_sp._CaT2 Methanothermobacter sp. CaT2] and [https://en.wikipedia.org/wiki/Methanothermobacter_wolfeii Methanothermobacter wolfeii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T61 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5T61 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=H2S:HYDROSULFURIC+ACID'>H2S</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MFN:N-[4,5,7-TRICARBOXYHEPTANOYL]-L-GAMMA-GLUTAMYL-N-{2-[4-({5-[(FORMYLAMINO)METHYL]-3-FURYL}METHOXY)PHENYL]ETHYL}-D-GLUTAMINE'>MFN</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=W:TUNGSTEN+ION'>W</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.55&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene></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=H2S:HYDROSULFURIC+ACID'>H2S</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=MFN:N-[4,5,7-TRICARBOXYHEPTANOYL]-L-GAMMA-GLUTAMYL-N-{2-[4-({5-[(FORMYLAMINO)METHYL]-3-FURYL}METHOXY)PHENYL]ETHYL}-D-GLUTAMINE'>MFN</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=W:TUNGSTEN+ION'>W</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Formylmethanofuran_dehydrogenase Formylmethanofuran dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.99.5 1.2.99.5] </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=5t61 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t61 OCA], [https://pdbe.org/5t61 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5t61 RCSB], [https://www.ebi.ac.uk/pdbsum/5t61 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5t61 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=5t61 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t61 OCA], [http://pdbe.org/5t61 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5t61 RCSB], [http://www.ebi.ac.uk/pdbsum/5t61 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5t61 ProSAT]</span></td></tr>
</table>
</table>
{{Large structure}}
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Biological methane formation starts with a challenging adenosine triphosphate (ATP)-independent carbon dioxide (CO2) fixation process. We explored this enzymatic process by solving the x-ray crystal structure of formyl-methanofuran dehydrogenase, determined here as Fwd(ABCDFG)2 and Fwd(ABCDFG)4 complexes, from Methanothermobacter wolfeii The latter 800-kilodalton apparatus consists of four peripheral catalytic sections and an electron-supplying core with 46 electronically coupled [4Fe-4S] clusters. Catalysis is separately performed by subunits FwdBD (FwdB and FwdD), which are related to tungsten-containing formate dehydrogenase, and subunit FwdA, a binuclear metal center carrying amidohydrolase. CO2 is first reduced to formate in FwdBD, which then diffuses through a 43-angstrom-long tunnel to FwdA, where it condenses with methanofuran to formyl-methanofuran. The arrangement of [4Fe-4S] clusters functions as an electron relay but potentially also couples the four tungstopterin active sites over 206 angstroms.
The methanogenic CO2 reducing-and-fixing enzyme is bifunctional and contains 46 [4Fe-4S] clusters.,Wagner T, Ermler U, Shima S Science. 2016 Oct 7;354(6308):114-117. PMID:27846502<ref>PMID:27846502</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5t61" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[SARS Coronavirus Main Proteinase|SARS Coronavirus Main Proteinase]]
*[[Virus protease 3D structures|Virus protease 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Formylmethanofuran dehydrogenase]]
[[Category: Large Structures]]
[[Category: Methanothermobacter sp. cat2]]
[[Category: Methanothermobacter sp. CaT2]]
[[Category: Methanothermobacter wolfeii]]
[[Category: Methanothermobacter wolfeii]]
[[Category: Ermler, U]]
[[Category: Ermler U]]
[[Category: Shima, S]]
[[Category: Shima S]]
[[Category: Wagner, T]]
[[Category: Wagner T]]
[[Category: Anaerobic]]
[[Category: Beta helicoidal]]
[[Category: Binuclear center]]
[[Category: Carboxylysine]]
[[Category: Channel]]
[[Category: Co2]]
[[Category: Co2 fixation]]
[[Category: Coupling]]
[[Category: Enzyme]]
[[Category: Ferredoxin]]
[[Category: Formate]]
[[Category: Formate dehydrogenase]]
[[Category: Formylmethanofuran]]
[[Category: Gate]]
[[Category: Green house gas]]
[[Category: Iron sulfur cluster]]
[[Category: Metallohydrolase]]
[[Category: Methanofuran]]
[[Category: Methanogenesis]]
[[Category: Nanomachine]]
[[Category: Oxidoreductase]]
[[Category: Tungsten]]
[[Category: Tungstopterin]]

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