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Structure paper

TitleStructural insights into the unusual core photocomplex from a triply extremophilic purple bacterium, Halorhodospira halochloris.
Journal, issue, pagesJ Integr Plant Biol, Year 2024
Publish dateFeb 27, 2024
AuthorsChen-Hui Qi / Guang-Lei Wang / Fang-Fang Wang / Jie Wang / Xiang-Ping Wang / Mei-Juan Zou / Fei Ma / Michael T Madigan / Yukihiro Kimura / Zheng-Yu Wang-Otomo / Long-Jiang Yu /
PubMed AbstractHalorhodospira (Hlr.) halochloris is a triply extremophilic phototrophic purple sulfur bacterium, as it is thermophilic, alkaliphilic, and extremely halophilic. The light-harvesting-reaction center ...Halorhodospira (Hlr.) halochloris is a triply extremophilic phototrophic purple sulfur bacterium, as it is thermophilic, alkaliphilic, and extremely halophilic. The light-harvesting-reaction center (LH1-RC) core complex of this bacterium displays an LH1-Q transition at 1,016 nm, which is the lowest-energy wavelength absorption among all known phototrophs. Here we report the cryo-EM structure of the LH1-RC at 2.42 Å resolution. The LH1 complex forms a tricyclic ring structure composed of 16 αβγ-polypeptides and one αβ-heterodimer around the RC. From the cryo-EM density map, two previously unrecognized integral membrane proteins, referred to as protein G and protein Q, were identified. Both of these proteins are single transmembrane-spanning helices located between the LH1 ring and the RC L-subunit and are absent from the LH1-RC complexes of all other purple bacteria of which the structures have been determined so far. Besides bacteriochlorophyll b molecules (B1020) located on the periplasmic side of the Hlr. halochloris membrane, there are also two arrays of bacteriochlorophyll b molecules (B800 and B820) located on the cytoplasmic side. Only a single copy of a carotenoid (lycopene) was resolved in the Hlr. halochloris LH1-α3β3 and this was positioned within the complex. The potential quinone channel should be the space between the LH1-α3β3 that accommodates the single lycopene but does not contain a γ-polypeptide, B800 and B820. Our results provide a structural explanation for the unusual Q red shift and carotenoid absorption in the Hlr. halochloris spectrum and reveal new insights into photosynthetic mechanisms employed by a species that thrives under the harshest conditions of any phototrophic microorganism known.
External linksJ Integr Plant Biol / PubMed:38411333
MethodsEM (single particle)
Resolution2.42 Å
Structure data

36907

8k5o

EMDB-36907, PDB-8k5o:
Cryo-EM structure of the RC-LH core comples from Halorhodospira halochloris
Method: EM (single particle) / Resolution: 2.42 Å

Chemicals

ChemComp-HEC:
HEME C / Heme C

ChemComp-PGV:
(1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL (11E)-OCTADEC-11-ENOATE / phospholipid*YM / Phosphatidylglycerol

ChemComp-LHG:
1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE / phospholipid*YM / Phosphatidylglycerol


PDB Unreleased entry

PDB-1lzm: Unknown entry

PDB-1lzp:
Unknown entry

ChemComp-UQ8:
Ubiquinone-8


ChemComp, No image

ChemComp-UNL:
Unknown ligand

ChemComp-FE:
Unknown entry / Iron

ChemComp-MQ8:
MENAQUINONE 8 / Vitamin K2

ChemComp-CDL:
CARDIOLIPIN / phospholipid*YM / Cardiolipin

ChemComp-LYC:
LYCOPENE / Lycopene

PDB-1lzq:
Crystal structure of the complex of mutant HIV-1 protease (A71V, V82T, I84V) with an ethylenamine peptidomimetic inhibitor BOC-PHE-PSI[CH2CH2NH]-PHE-GLU-PHE-NH2

ChemComp-PEF:
DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE / phospholipid*YM / Phosphatidylethanolamine

ChemComp-BGL:
2-O-octyl-beta-D-glucopyranose / detergent*YM

Source
  • halorhodospira halochloris (bacteria)
KeywordsPHOTOSYNTHESIS / RC-LH complex / HALORHODOSPIRA HALOCHLORIS

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