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SOLUTION STRUCTURE OF THE NADP(H) BINDING COMPONENT (DIII) OF PROTON-TRANSLOCATING TRANSHYDROGENASE FROM RHODOSPIRILLUM RUBRUMSOLUTION STRUCTURE OF THE NADP(H) BINDING COMPONENT (DIII) OF PROTON-TRANSLOCATING TRANSHYDROGENASE FROM RHODOSPIRILLUM RUBRUM
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedTranshydrogenase 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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