2WJN
Lipidic sponge phase crystal structure of photosynthetic reaction centre from Blastochloris viridis (high dose)
Summary for 2WJN
| Entry DOI | 10.2210/pdb2wjn/pdb |
| Related | 1DXR 1PRC 1R2C 1VRN 2JBL 2PRC 2WJM 3PRC 5PRC 6PRC 7PRC |
| Descriptor | PHOTOSYNTHETIC REACTION CENTER CYTOCHROME C SUBUNIT, MENAQUINONE-7, 15-cis-1,2-dihydroneurosporene, ... (12 entities in total) |
| Functional Keywords | bacteriochlorophyll, lipidic-sponge phase, photosynthesis, reaction center, electron transport, cell membrane, metal-binding, transmembrane, formylation, chromophore, chlorophyll, lipoprotein, iron, heme, lipids, membrane, transport, magnesium |
| Biological source | RHODOPSEUDOMONAS VIRIDIS More |
| Total number of polymer chains | 4 |
| Total formula weight | 142873.67 |
| Authors | Wohri, A.B.,Wahlgren, W.Y.,Malmerberg, E.,Johansson, L.C.,Neutze, R.,Katona, G. (deposition date: 2009-05-27, release date: 2009-09-22, Last modification date: 2024-10-16) |
| Primary citation | Wohri, A.B.,Wahlgren, W.Y.,Malmerberg, E.,Johansson, L.C.,Neutze, R.,Katona, G. Lipidic sponge phase crystal structure of a photosynthetic reaction center reveals lipids on the protein surface. Biochemistry, 48:9831-9838, 2009 Cited by PubMed 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. PubMed: 19743880DOI: 10.1021/bi900545e PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.86 Å) |
Structure validation
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