The solution structure of the PufX polypeptide from Rhodobacter sphaeroides |
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Authors: | Tunnicliffe Richard B Ratcliffe Emma C Hunter C Neil Williamson Mike P |
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Affiliation: | Department of Molecular Biology and Biotechnology, University of Sheffield, Firth Court, Western Bank, Sheffield S10 2TN, UK. |
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Abstract: | PufX organises the photosynthetic reaction centre–light harvesting complex 1 (RC–LH1) core complex of Rhodobacter sphaeroides and facilitates quinol/quinone exchange between the RC and cytochrome bc1 complexes. The structure of PufX in organic solvent reveals two hydrophobic helices flanked by unstructured termini and connected by a helical bend. The proposed location of basic residues and tryptophans at the membrane interface orients the C-terminal helix along the membrane normal, with the GXXXG motifs in positions unsuitable as direct drivers of dimerisation of the RC–LH1 complex. The N-terminal helix is predicted to extend 40 Å along the membrane interface. |
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Keywords: | Photosynthesis Reaction centre NMR structure Light harvesting Membrane protein Rhodobacter sphaeroides |
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