6ET5
Reaction centre light harvesting complex 1 from Blc. virids
Summary for 6ET5
| Entry DOI | 10.2210/pdb6et5/pdb |
| EMDB information | 3951 |
| Descriptor | Photosynthetic reaction center cytochrome c subunit, BACTERIOPHEOPHYTIN B, Ubiquinone-9, ... (17 entities in total) |
| Functional Keywords | reaction centre light harvesting complex 1 blc. viridis cryo-em rc-lh1 photosynthesis, photosynthesis |
| Biological source | Blastochloris viridis (Rhodopseudomonas viridis) More |
| Total number of polymer chains | 54 |
| Total formula weight | 454562.09 |
| Authors | Qian, P.,Siebert, C.A.,Canniffe, D.P.,Wang, P.,Hunter, C.N. (deposition date: 2017-10-25, release date: 2018-04-11, Last modification date: 2025-04-09) |
| Primary citation | Qian, P.,Siebert, C.A.,Wang, P.,Canniffe, D.P.,Hunter, C.N. Cryo-EM structure of the Blastochloris viridis LH1-RC complex at 2.9 angstrom. Nature, 556:203-208, 2018 Cited by PubMed Abstract: The light-harvesting 1-reaction centre (LH1-RC) complex is a key functional component of bacterial photosynthesis. Here we present a 2.9 Å resolution cryo-electron microscopy structure of the bacteriochlorophyll b-based LH1-RC complex from Blastochloris viridis that reveals the structural basis for absorption of infrared light and the molecular mechanism of quinone migration across the LH1 complex. The triple-ring LH1 complex comprises a circular array of 17 β-polypeptides sandwiched between 17 α- and 16 γ-polypeptides. Tight packing of the γ-apoproteins between β-polypeptides collectively interlocks and stabilizes the LH1 structure; this, together with the short Mg-Mg distances of bacteriochlorophyll b pairs, contributes to the large redshift of bacteriochlorophyll b absorption. The 'missing' 17th γ-polypeptide creates a pore in the LH1 ring, and an adjacent binding pocket provides a folding template for a quinone, Q , which adopts a compact, export-ready conformation before passage through the pore and eventual diffusion to the cytochrome bc complex. PubMed: 29618818DOI: 10.1038/s41586-018-0014-5 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.87 Å) |
Structure validation
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