6Z5R

RC-LH1(16) complex from Rhodopseudomonas palustris

Summary for 6Z5R

• Entry DOI: 10.2210/pdb6z5r/pdb
• EMDB information: 11080
• Descriptor: Light-harvesting complex 1 alpha chain, DODECYL-BETA-D-MALTOSIDE, BACTERIOPHEOPHYTIN A, ... (16 entities in total)
• Functional Keywords: reaction center, light harvesting, protein w, quinone, photosynthesis
• Biological source: Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009); More
• Total number of polymer chains: 35
• Total formula weight: 362475.63

Authors

Swainsbury, D.J.K.,Qian, P.,Hitchcock, A.,Hunter, C.N. (deposition date: 2020-05-27, release date: 2021-01-13, Last modification date: 2024-10-23)

Primary citation

Swainsbury, D.J.K.,Qian, P.,Jackson, P.J.,Faries, K.M.,Niedzwiedzki, D.M.,Martin, E.C.,Farmer, D.A.,Malone, L.A.,Thompson, R.F.,Ranson, N.A.,Canniffe, D.P.,Dickman, M.J.,Holten, D.,Kirmaier, C.,Hitchcock, A.,Hunter, C.N.
Structures of Rhodopseudomonas palustris RC-LH1 complexes with open or closed quinone channels.
Sci Adv, 7:-, 2021

PubMed Abstract: The reaction-center light-harvesting complex 1 (RC-LH1) is the core photosynthetic component in purple phototrophic bacteria. We present two cryo-electron microscopy structures of RC-LH1 complexes from A 2.65-Å resolution structure of the RC-LH1-W complex consists of an open 14-subunit LH1 ring surrounding the RC interrupted by protein-W, whereas the complex without protein-W at 2.80-Å resolution comprises an RC completely encircled by a closed, 16-subunit LH1 ring. Comparison of these structures provides insights into quinone dynamics within RC-LH1 complexes, including a previously unidentified conformational change upon quinone binding at the RC Q site, and the locations of accessory quinone binding sites that aid their delivery to the RC. The structurally unique protein-W prevents LH1 ring closure, creating a channel for accelerated quinone/quinol exchange.

PubMed: 33523887
DOI: 10.1126/sciadv.abe2631

Experimental method

ELECTRON MICROSCOPY (2.8 Å)