1E3T

Solution Structure of the NADP(H) binding Component (dIII) of Proton-Translocating Transhydrogenase from Rhodospirillum rubrum

Summary for 1E3T

• Entry DOI: 10.2210/pdb1e3t/pdb
• Descriptor: NICOTINAMIDE NUCLEOTIDE TRANSHYDROGENASE (SUBUNIT BETA), NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (2 entities in total)
• Functional Keywords: transhydrogenase, membrane protein, proton translocation, nucleotide binding
• Biological source: RHODOSPIRILLUM RUBRUM
• Total number of polymer chains: 1
• Total formula weight: 22228.91

Authors

Jeeves, M.,Smith, K.J.,Quirk, P.G.,Cotton, N.P.J.,Jackson, J.B. (deposition date: 2000-06-22, release date: 2000-10-03, Last modification date: 2024-05-15)

Primary citation

Jeeves, M.,Smith, K.J.,Quirk, P.G.,Cotton, N.P.J.,Jackson, J.B.
Solution Structure of the Nadp(H)-Binding Component (Diii) of Proton-Translocating Transhydrogenase from Rhodospirillum Rubrum
Biochim.Biophys.Acta, 1459:248-, 2000

PubMed 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 beta-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 betaalphabetaalphabeta 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.

PubMed: 11004437
DOI: 10.1016/S0005-2728(00)00159-6

Experimental method

SOLUTION NMR