Abstract
X-ray crystallography has shown that the Rhodobacter sphaeroides reaction centre engages in a specific interaction with a molecule of the anionic phospholipid (diphosphatidyl glycerol). We have used extensive sequence alignments to determine the degree to which the residues that interact with the are conserved in other species of photosynthetic bacteria with this type of reaction centre. We discuss the possibility that this cardiolipin binding site is a conserved feature of these reaction centres. We also discuss the cross-species conservation of residues involved in lipid binding in a recently-reported X-ray crystal structure for the reaction centre from Thermochromatium tepidum, and compare the structure of this reaction centre with the complex from Rhodobacter sphaeroides.
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