6T8Z
NAD+-dependent fungal formate dehydrogenase from Chaetomium thermophilum: A ternary complex with the oxidised form of the cofactor NAD+ and the substrate formate both at a primary and secondary sites.
This is a non-PDB format compatible entry.
Summary for 6T8Z
| Entry DOI | 10.2210/pdb6t8z/pdb |
| Related | 6T8Y |
| Descriptor | Formate dehydrogenase, DI(HYDROXYETHYL)ETHER, FORMIC ACID, ... (6 entities in total) |
| Functional Keywords | nad+ dependent formate dehydrogenase, cytosolic protein |
| Biological source | Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) |
| Total number of polymer chains | 4 |
| Total formula weight | 186764.81 |
| Authors | Isupov, M.N.,Yelmazer, B.,De Rose, S.A.,Littlechild, J.A. (deposition date: 2019-10-25, release date: 2020-11-18, Last modification date: 2024-01-24) |
| Primary citation | Yilmazer, B.,Isupov, M.N.,De Rose, S.A.,Bulut, H.,Benninghoff, J.C.,Binay, B.,Littlechild, J.A. Structural insights into the NAD + -dependent formate dehydrogenase mechanism revealed from the NADH complex and the formate NAD + ternary complex of the Chaetomium thermophilum enzyme. J.Struct.Biol., 212:107657-107657, 2020 Cited by PubMed Abstract: The removal of carbon dioxide from the waste streams of industrial processes is a major challenge for creation of a sustainable circular economy. This makes the synthesis of formate from CO by NAD dependent formate dehydrogenases (FDHs) an attractive process for this purpose. The efficiency of this reaction is however low and to achieve a viable industrial process an optimised engineered enzyme needs to be developed. In order to understand the detailed enzymatic mechanism of catalysis structures of different cofactor and substrate complexes of the FDH from the thermophilic filamentous fungus, Chaetomium thermophilum have been determined to 1.2-1.3 Å resolution. The substrate formate is shown to be held by four hydrogen bonds in the FDH catalytic site within the ternary complex with substrate and NADand a secondary formate binding site is observed in crystals soaked with substrate. Water molecules are excluded from the FDH catalytic site when the substrate is bound. The angle between the plane of the NAD cofactor pyridine ring and the plane of the formate molecule is around 27°. Additionally, structures of a FDH mutant enzyme, N120C, in complex with the reduced form of the cofactor have also been determined both in the presence and absence of formate bound at the secondary site. These structures provide further understanding of the catalytic mechanism of this fungal enzyme. PubMed: 33148525DOI: 10.1016/j.jsb.2020.107657 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.21 Å) |
Structure validation
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