5KMS
The structure of type II NADH dehydrogenase from Caldalkalibacillus thermarum complexed with NAD+ at 2.5 angstrom resolution.
Summary for 5KMS
| Entry DOI | 10.2210/pdb5kms/pdb |
| Related | 5KMP 5KMQ 5KMR |
| Descriptor | FAD-dependent pyridine nucleotide-disulfide oxidoreductase, FLAVIN-ADENINE DINUCLEOTIDE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (4 entities in total) |
| Functional Keywords | rossmann fold, nadh dehydrogenase, oxidoreductase |
| Biological source | Caldalkalibacillus thermarum TA2.A1 |
| Total number of polymer chains | 4 |
| Total formula weight | 182093.58 |
| Authors | Cook, G.M.,Aragao, D.,Nakatani, Y. (deposition date: 2016-06-27, release date: 2017-02-01, Last modification date: 2023-10-25) |
| Primary citation | Blaza, J.N.,Bridges, H.R.,Aragao, D.,Dunn, E.A.,Heikal, A.,Cook, G.M.,Nakatani, Y.,Hirst, J. The mechanism of catalysis by type-II NADH:quinone oxidoreductases. Sci Rep, 7:40165-40165, 2017 Cited by PubMed Abstract: Type II NADH:quinone oxidoreductase (NDH-2) is central to the respiratory chains of many organisms. It is not present in mammals so may be exploited as an antimicrobial drug target or used as a substitute for dysfunctional respiratory complex I in neuromuscular disorders. NDH-2 is a single-subunit monotopic membrane protein with just a flavin cofactor, yet no consensus exists on its mechanism. Here, we use steady-state and pre-steady-state kinetics combined with mutagenesis and structural studies to determine the mechanism of NDH-2 from Caldalkalibacillus thermarum. We show that the two substrate reactions occur independently, at different sites, and regardless of the occupancy of the partner site. We conclude that the reaction pathway is determined stochastically, by the substrate/product concentrations and dissociation constants, and can follow either a ping-pong or ternary mechanism. This mechanistic versatility provides a unified explanation for all extant data and a new foundation for the development of therapeutic strategies. PubMed: 28067272DOI: 10.1038/srep40165 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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