7VW6
Cryo-EM Structure of Formate Dehydrogenase 1 from Methylorubrum extorquens AM1
Summary for 7VW6
| Entry DOI | 10.2210/pdb7vw6/pdb |
| EMDB information | 32151 |
| Descriptor | Formate dehydrogenase, Tungsten-containing formate dehydrogenase beta subunit, IRON/SULFUR CLUSTER, ... (8 entities in total) |
| Functional Keywords | complex, oxidoreductase |
| Biological source | Methylorubrum extorquens AM1 More |
| Total number of polymer chains | 2 |
| Total formula weight | 173741.01 |
| Authors | Yoshikawa, T.,Makino, F.,Miyata, T.,Suzuki, Y.,Tanaka, H.,Namba, K.,Sowa, K.,Kitazumi, Y.,Shirai, O. (deposition date: 2021-11-09, release date: 2022-06-01, Last modification date: 2024-06-26) |
| Primary citation | Yoshikawa, T.,Makino, F.,Miyata, T.,Suzuki, Y.,Tanaka, H.,Namba, K.,Kano, K.,Sowa, K.,Kitazumi, Y.,Shirai, O. Multiple electron transfer pathways of tungsten-containing formate dehydrogenase in direct electron transfer-type bioelectrocatalysis. Chem.Commun.(Camb.), 58:6478-6481, 2022 Cited by PubMed Abstract: Tungsten-containing formate dehydrogenase from AM1 (FoDH1)-a promising biocatalyst for the interconversion of carbon dioxide/formate and nicotine adenine dinucleotide (NAD)/NADH redox couples-was investigated using structural biology and bioelectrochemistry. FoDH1 is reported to be an enzyme that can realize "direct electron transfer (DET)-type bioelectrocatalysis." However, its 3-D structure, electrode-active sites, and electron transfer (ET) pathways remain unclear. The ET pathways were investigated using structural information, electrostatic interactions between the electrode and the enzyme, and the differences in the substrates. Two electrode-active sites and multiple ET pathways in FoDH1 were discovered. PubMed: 35535582DOI: 10.1039/d2cc01541b PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.19 Å) |
Structure validation
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