5T5M
TUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE FROM METHANOTHERMOBACTER WOLFEII, TRIGONAL FORM AT 2.5 A.
Summary for 5T5M
| Entry DOI | 10.2210/pdb5t5m/pdb |
| Descriptor | Tungsten formylmethanofuran dehydrogenase subunit fwdA, POTASSIUM ION, IRON/SULFUR CLUSTER, ... (15 entities in total) |
| Functional Keywords | co2 fixation, metallohydrolase, formate dehydrogenase, tungstopterin, methanogenesis, green house gas, methanothermobacter wolfeii, iron sulfur cluster, ferredoxin, beta helicoidal, channel, formate, co2, methanofuran, formylmethanofuran, nanomachine, binuclear center, tungsten, gate, coupling, enzyme, anaerobic, carboxylysine, oxidoreductase |
| Biological source | Methanothermobacter wolfeii More |
| Total number of polymer chains | 6 |
| Total formula weight | 207509.91 |
| Authors | Wagner, T.,Ermler, U.,Shima, S. (deposition date: 2016-08-31, release date: 2016-10-19, Last modification date: 2024-01-17) |
| Primary citation | Wagner, T.,Ermler, U.,Shima, S. The methanogenic CO2 reducing-and-fixing enzyme is bifunctional and contains 46 [4Fe-4S] clusters. Science, 354:114-117, 2016 Cited by PubMed Abstract: Biological methane formation starts with a challenging adenosine triphosphate (ATP)-independent carbon dioxide (CO) fixation process. We explored this enzymatic process by solving the x-ray crystal structure of formyl-methanofuran dehydrogenase, determined here as Fwd(ABCDFG) and Fwd(ABCDFG) 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. CO 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. PubMed: 27846502DOI: 10.1126/science.aaf9284 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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