1e3t
From Proteopedia
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SOLUTION STRUCTURE OF THE NADP(H) BINDING COMPONENT (DIII) OF PROTON-TRANSLOCATING TRANSHYDROGENASE FROM RHODOSPIRILLUM RUBRUM
Overview
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.
About this Structure
1E3T is a Single protein structure of sequence from Rhodospirillum rubrum with NAP as ligand. Active as NAD(P)(+) transhydrogenase (B-specific), with EC number 1.6.1.1 Full crystallographic information is available from OCA.
Reference
Solution structure of the NADP(H)-binding component (dIII) of proton-translocating transhydrogenase from Rhodospirillum rubrum., Jeeves M, Smith KJ, Quirk PG, Cotton NP, Jackson JB, Biochim Biophys Acta. 2000 Aug 15;1459(2-3):248-57. PMID:11004437
Page seeded by OCA on Tue Nov 20 13:45:53 2007
