5t5m
From Proteopedia
(Difference between revisions)
Line 9: | Line 9: | ||
<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=5t5m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t5m OCA], [http://pdbe.org/5t5m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5t5m RCSB], [http://www.ebi.ac.uk/pdbsum/5t5m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5t5m 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=5t5m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t5m OCA], [http://pdbe.org/5t5m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5t5m RCSB], [http://www.ebi.ac.uk/pdbsum/5t5m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5t5m ProSAT]</span></td></tr> | ||
</table> | </table> | ||
+ | <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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 5t5m" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> |
Revision as of 14:54, 22 December 2016
TUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE FROM METHANOTHERMOBACTER WOLFEII, TRIGONAL FORM AT 2.5 A.
|
Categories: Formylmethanofuran dehydrogenase | Methanothermobacter wolfeii | Ermler, U | Shima, S | Wagner, T | Anaerobic | Beta helicoidal | Binuclear center | Carboxylysine | Channel | Co2 | Co2 fixation | Coupling | Enzyme | Ferredoxin | Formate | Formate dehydrogenase | Formylmethanofuran | Gate | Green house gas | Iron sulfur cluster | Metallohydrolase | Methanofuran | Methanogenesis | Nanomachine | Oxidoreductase | Tungsten | Tungstopterin