7VY3

STRUCTURE OF PHOTOSYNTHETIC LH1-RC SUPER-COMPLEX OF RHODOBACTER SPHAEROIDES LACKING PROTEIN-U

Summary for 7VY3

• Entry DOI: 10.2210/pdb7vy3/pdb
• EMDB information: 32193
• Descriptor: Photosynthetic reaction center L subunit, (1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL (11E)-OCTADEC-11-ENOATE, LAURYL DIMETHYLAMINE-N-OXIDE, ... (16 entities in total)
• Functional Keywords: lh1-rc complex, photosynthesis, purple bacteria
• Biological source: Rhodobacter sphaeroides f. sp. denitrificans; More
• Total number of polymer chains: 25
• Total formula weight: 288908.91

Authors

Tani, K.,Kanno, R.,Kawamura, S.,Kikuchi, R.,Nagashima, K.V.P.,Hall, M.,Takahashi, A.,Yu, L.-J.,Kimura, Y.,Madigan, M.T.,Mizoguchi, A.,Humbel, B.M.,Wang-Otomo, Z.-Y. (deposition date: 2021-11-13, release date: 2022-04-27)

Primary citation

Tani, K.,Kanno, R.,Kikuchi, R.,Kawamura, S.,Nagashima, K.V.P.,Hall, M.,Takahashi, A.,Yu, L.J.,Kimura, Y.,Madigan, M.T.,Mizoguchi, A.,Humbel, B.M.,Wang-Otomo, Z.Y.
Asymmetric structure of the native Rhodobacter sphaeroides dimeric LH1-RC complex.
Nat Commun, 13:1904-1904, 2022

PubMed Abstract: Rhodobacter sphaeroides is a model organism in bacterial photosynthesis, and its light-harvesting-reaction center (LH1-RC) complex contains both dimeric and monomeric forms. Here we present cryo-EM structures of the native LH1-RC dimer and an LH1-RC monomer lacking protein-U (ΔU). The native dimer reveals several asymmetric features including the arrangement of its two monomeric components, the structural integrity of protein-U, the overall organization of LH1, and rigidities of the proteins and pigments. PufX plays a critical role in connecting the two monomers in a dimer, with one PufX interacting at its N-terminus with another PufX and an LH1 β-polypeptide in the other monomer. One protein-U was only partially resolved in the dimeric structure, signaling different degrees of disorder in the two monomers. The ΔU LH1-RC monomer was half-moon-shaped and contained 11 α- and 10 β-polypeptides, indicating a critical role for protein-U in controlling the number of αβ-subunits required for dimer assembly and stabilization. These features are discussed in relation to membrane topology and an assembly model proposed for the native dimeric complex.

PubMed: 35393413
DOI: 10.1038/s41467-022-29453-8

Experimental method

ELECTRON MICROSCOPY (2.63 Å)