Abstract：
:Membrane proteins are embedded in a lipid bilayer and maintain strong interactions with lipid molecules. Tightly bound lipids are responsible for vertical positioning and integration of proteins in the membrane and for assembly of multisubunit complexes and occasionally act as substrates. In this work we present the lipidic sponge phase crystal structure of the reaction center from Blastochloris viridis to 1.86 A, which reveals lipid molecules interacting with the protein surface. A diacylglycerol molecule is bound, through a thioether bond, to the N-terminus of the tetraheme cytochrome c subunit. From the electron density recovered at the Q(B) site and the observed change in recombination kinetics in lipidic sponge phase-grown crystals, the mobile ubiquinone appears to be displaced by a monoolein molecule. A 36 A long electron density feature is observed at the interface of transmembrane helices belonging to the H- and M-subunits, probably arising from an unidentified lipid.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Wöhri AB,Wahlgren WY,Malmerberg E,Johansson LC,Neutze R,Katona Gdoi
10.1021/bi900545esubject
Has Abstractpub_date
2009-10-20 00:00:00pages
9831-8issue
41eissn
0006-2960issn
1520-4995journal_volume
48pub_type
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