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The solution structure of the PufX polypeptide from Rhodobacter sphaeroides
Author(s) -
Tunnicliffe Richard B.,
Ratcliffe Emma C.,
Hunter C. Neil,
Williamson Mike P.
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.11.065
Subject(s) - rhodobacter sphaeroides , helix (gastropod) , chemistry , rhodospirillaceae , crystallography , photosynthetic reaction centre , photosynthesis , rhodobacter , membrane , cytochrome c , biophysics , stereochemistry , biochemistry , biology , mutant , ecology , snail , gene , mitochondrion
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 bc 1 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.