7DDQ
Structure of RC-LH1-PufX from Rhodobacter veldkampii
Summary for 7DDQ
| Entry DOI | 10.2210/pdb7ddq/pdb |
| EMDB information | 30656 |
| Descriptor | Antenna pigment protein alpha chain, BACTERIOPHEOPHYTIN A, FE (III) ION, ... (12 entities in total) |
| Functional Keywords | membrane protein, light-harvesting, reaction center, pufx, photosynthesis |
| Biological source | Rhodobacter veldkampii DSM 11550 More |
| Total number of polymer chains | 34 |
| Total formula weight | 335120.87 |
| Authors | Bracun, L.,Yamagata, A.,Shirouzu, M.,Liu, L.N. (deposition date: 2020-10-29, release date: 2021-06-30, Last modification date: 2025-06-25) |
| Primary citation | Bracun, L.,Yamagata, A.,Christianson, B.M.,Terada, T.,Canniffe, D.P.,Shirouzu, M.,Liu, L.N. Cryo-EM structure of the photosynthetic RC-LH1-PufX supercomplex at 2.8-angstrom resolution. Sci Adv, 7:-, 2021 Cited by PubMed Abstract: The reaction center (RC)-light-harvesting complex 1 (LH1) supercomplex plays a pivotal role in bacterial photosynthesis. Many RC-LH1 complexes integrate an additional protein PufX that is key for bacterial growth and photosynthetic competence. Here, we present a cryo-electron microscopy structure of the RC-LH1-PufX supercomplex from at 2.8-Å resolution. The RC-LH1-PufX monomer contains an LH ring of 15 αβ-polypeptides with a 30-Å gap formed by PufX. PufX acts as a molecular "cross brace" to reinforce the RC-LH1 structure. The unusual PufX-mediated large opening in the LH1 ring and defined arrangement of proteins and cofactors provide the molecular basis for the assembly of a robust RC-LH1-PufX supercomplex and efficient quinone transport and electron transfer. These architectural features represent the natural strategies for anoxygenic photosynthesis and environmental adaptation. PubMed: 34134992DOI: 10.1126/sciadv.abf8864 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.84 Å) |
Structure validation
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