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- W1992495893 abstract "Transhydrogenase is a proton pump found in the membranes of bacteria and animal mitochondria. The solution structure of the expressed, 21.5 kDa, NADP(H)-binding component (dIII) of transhydrogenase from Rhodospirillum rubrum has been solved by NMR methods. This is the first description of the structure of dIII from a bacterial source. The protein adopts a Rossmann fold: an open, twisted, parallel β-sheet, flanked by helices. However, the binding of NADP+ to dIII is profoundly different to that seen in other Rossmann structures, in that its orientation is reversed: the adenosine moiety interacts with the first βαβαβ motif, and the nicotinamide with the second. Features in the structure that might be responsible for changes in nucleotide-binding affinity during catalysis, and for interaction with other components of the enzyme, are identified. The results are compared with the recently determined, high-resolution crystal structures of human and bovine dIII which also show the reversed nucleotide orientation." @default.
- W1992495893 created "2016-06-24" @default.
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- W1992495893 date "2000-08-01" @default.
- W1992495893 modified "2023-09-25" @default.
- W1992495893 title "Solution structure of the NADP(H)-binding component (dIII) of proton-translocating transhydrogenase from Rhodospirillum rubrum" @default.
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- W1992495893 doi "https://doi.org/10.1016/s0005-2728(00)00159-6" @default.
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