Conservation of lipid functions in cytochrome bc complexes.

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TitleConservation of lipid functions in cytochrome bc complexes.
Publication TypeJournal Article
Year of Publication2011
AuthorsS Hasan, S, Yamashita, E, Ryan, CM, Whitelegge, JP, Cramer, WA
JournalJ Mol Biol
Date Published2011 Nov 18
Keywordsbeta Carotene, Binding Sites, Chlorophyll, Chlorophyll A, Crystallography, X-Ray, Cyanobacteria, Cytochrome b6f Complex, Electron Transport Complex III, Lipids, Models, Molecular, Protein Conformation

Lipid binding sites and properties are compared in two sub-families of hetero-oligomeric membrane protein complexes known to have similar functions in order to gain further understanding of the role of lipid in the function, dynamics, and assembly of these complexes. Using the crystal structure information for both complexes, we compared the lipid binding properties of the cytochrome b(6)f and bc(1) complexes that function in photosynthetic and respiratory membrane energy transduction. Comparison of lipid and detergent binding sites in the b(6)f complex with those in bc(1) shows significant conservation of lipid positions. Seven lipid binding sites in the cyanobacterial b(6)f complex overlap three natural sites in the Chlamydomonas reinhardtii algal complex and four sites in the yeast mitochondrial bc(1) complex. The specific identity of lipids is different in b(6)f and bc(1) complexes: b(6)f contains sulfoquinovosyldiacylglycerol, phosphatidylglycerol, phosphatidylcholine, monogalactosyldiacylglycerol, and digalactosyldiacylglycerol, whereas cardiolipin, phosphatidylethanolamine, and phosphatidic acid are present in the yeast bc(1) complex. The lipidic chlorophyll a and β-carotene (β-car) in cyanobacterial b(6)f, as well as eicosane in C. reinhardtii, are unique to the b(6)f complex. Inferences of lipid binding sites and functions were supported by sequence, interatomic distance, and B-factor information on interacting lipid groups and coordinating amino acid residues. The lipid functions inferred in the b(6)f complex are as follows: (i) substitution of a transmembrane helix by a lipid and chlorin ring, (ii) lipid and β-car connection of peripheral and core domains, (iii) stabilization of the iron-sulfur protein transmembrane helix, (iv) n-side charge and polarity compensation, and (v) β-car-mediated super-complex with the photosystem I complex.

Alternate JournalJ. Mol. Biol.
PubMed ID21978667
PubMed Central IDPMC3215850
Grant ListGM-088499 / GM / NIGMS NIH HHS / United States
R01 GM038323-23 / GM / NIGMS NIH HHS / United States
GM-038323 / GM / NIGMS NIH HHS / United States
R56 GM038323 / GM / NIGMS NIH HHS / United States
P50 GM088499 / GM / NIGMS NIH HHS / United States
R01 GM038323 / GM / NIGMS NIH HHS / United States