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TitleAn LH1-RC photocomplex from an extremophilic phototroph provides insight into origins of two photosynthesis proteins.
Journal, issue, pagesCommun Biol, Vol. 5, Issue 1, Page 1197, Year 2022
Publish dateNov 7, 2022
AuthorsKazutoshi Tani / Ryo Kanno / Keigo Kurosawa / Shinichi Takaichi / Kenji V P Nagashima / Malgorzata Hall / Long-Jiang Yu / Yukihiro Kimura / Michael T Madigan / Akira Mizoguchi / Bruno M Humbel / Zheng-Yu Wang-Otomo /
PubMed AbstractRhodopila globiformis is the most acidophilic of anaerobic purple phototrophs, growing optimally in culture at pH 5. Here we present a cryo-EM structure of the light-harvesting 1-reaction center (LH1- ...Rhodopila globiformis is the most acidophilic of anaerobic purple phototrophs, growing optimally in culture at pH 5. Here we present a cryo-EM structure of the light-harvesting 1-reaction center (LH1-RC) complex from Rhodopila globiformis at 2.24 Å resolution. All purple bacterial cytochrome (Cyt, encoded by the gene pufC) subunit-associated RCs with known structures have their N-termini truncated. By contrast, the Rhodopila globiformis RC contains a full-length tetra-heme Cyt with its N-terminus embedded in the membrane forming an α-helix as the membrane anchor. Comparison of the N-terminal regions of the Cyt with PufX polypeptides widely distributed in Rhodobacter species reveals significant structural similarities, supporting a longstanding hypothesis that PufX is phylogenetically related to the N-terminus of the RC-bound Cyt subunit and that a common ancestor of phototrophic Proteobacteria contained a full-length tetra-heme Cyt subunit that evolved independently through partial deletions of its pufC gene. Eleven copies of a novel γ-like polypeptide were also identified in the bacteriochlorophyll a-containing Rhodopila globiformis LH1 complex; γ-polypeptides have previously been found only in the LH1 of bacteriochlorophyll b-containing species. These features are discussed in relation to their predicted functions of stabilizing the LH1 structure and regulating quinone transport under the warm acidic conditions.
External linksCommun Biol / PubMed:36344631 / PubMed Central
MethodsEM (single particle)
Resolution2.24 Å
Structure data

33501

7xxf

EMDB-33501, PDB-7xxf:
Structure of photosynthetic LH1-RC super-complex of Rhodopila globiformis
Method: EM (single particle) / Resolution: 2.24 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-BCL:
BACTERIOCHLOROPHYLL A / Bacteriochlorophyll

ChemComp-BPH:
BACTERIOPHEOPHYTIN A / Pheophytin

ChemComp-U10:
UBIQUINONE-10 / Coenzyme Q10

ChemComp-LMT:
DODECYL-BETA-D-MALTOSIDE / detergent*YM

ChemComp-FE:
Unknown entry / Iron

ChemComp-MQ9:
MENAQUINONE-9 / Vitamin K2

ChemComp-I7D:
(6~{E},8~{E},10~{E},12~{E},14~{E},16~{E},18~{E},20~{E},22~{E},24~{E},26~{E},28~{E})-2,31-dimethoxy-2,6,10,14,19,23,27,31-octamethyl-dotriaconta-6,8,10,12,14,16,18,20,22,24,26,28-dodecaen-5-one

ChemComp-CDL:
CARDIOLIPIN / phospholipid*YM / Cardiolipin

ChemComp-PEE:
1,2-dioleoyl-sn-glycero-3-phosphoethanolamine / DOPE, phospholipid*YM / Discrete optimized protein energy

ChemComp-HOH:
WATER / Water

Source
  • rhodopila globiformis (bacteria)
KeywordsPHOTOSYNTHESIS / LH1-RC COMPLEX / PURPLE BACTERIA

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