8YGL
Rhodobacter blasticus RC-LH1 monomer
Summary for 8YGL
| Entry DOI | 10.2210/pdb8ygl/pdb |
| EMDB information | 39255 |
| Descriptor | Antenna pigment protein beta chain, CARDIOLIPIN, BACTERIOPHEOPHYTIN A, ... (13 entities in total) |
| Functional Keywords | photosynthesis, light-harvesting complex |
| Biological source | Fuscovulum blasticum DSM 2131 More |
| Total number of polymer chains | 34 |
| Total formula weight | 361517.51 |
| Authors | Liu, L.N.,Zhang, Y.Z.,Wang, P.,Christianson, B.M.,Ugurlar, D. (deposition date: 2024-02-26, release date: 2025-03-05) |
| Primary citation | Wang, P.,Christianson, B.M.,Ugurlar, D.,Mao, R.,Zhang, Y.,Liu, Z.K.,Zhang, Y.Y.,Gardner, A.M.,Gao, J.,Zhang, Y.Z.,Liu, L.N. Architectures of photosynthetic RC-LH1 supercomplexes from Rhodobacter blasticus. Sci Adv, 10:eadp6678-eadp6678, 2024 Cited by PubMed Abstract: The reaction center-light-harvesting complex 1 (RC-LH1) plays an essential role in the primary reactions of bacterial photosynthesis. Here, we present high-resolution structures of native monomeric and dimeric RC-LH1 supercomplexes from () using cryo-electron microscopy. The RC-LH1 monomer is composed of an RC encircled by an open LH1 ring comprising 15 αβ heterodimers and a PufX transmembrane polypeptide. In the RC-LH1 dimer, two crossing PufX polypeptides mediate dimerization. Unlike counterpart, RC-LH1 dimer has a less bent conformation, lacks the PufY subunit near the LH1 opening, and includes two extra LH1 αβ subunits, forming a more enclosed S-shaped LH1 ring. Spectroscopic assays reveal that these unique structural features are accompanied by changes in the kinetics of quinone/quinol trafficking between RC-LH1 and cytochrome . Our findings reveal the assembly principles and structural variability of photosynthetic RC-LH1 supercomplexes, highlighting diverse strategies used by phototrophic bacteria to optimize light-harvesting and electron transfer in competitive environments. PubMed: 39383221DOI: 10.1126/sciadv.adp6678 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.6 Å) |
Structure validation
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