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TitleStructure and Biochemistry of the LH1-RC Photocomplex from the Halophilic Purple Bacterium, .
Journal, issue, pagesBiochemistry, Vol. 64, Issue 14, Page 3070-3080, Year 2025
Publish dateJul 15, 2025
AuthorsKazutoshi Tani / Ryo Kanno / Miyu Inami / Takumi Ooya / Ryo Matsushita / Kazuki Inada / Shinji Takenaka / Shinichi Takaichi / Endang R Purba / Malgorzata Hall / Toshiaki Mochizuki / Long-Jiang Yu / Akira Mizoguchi / Bruno M Humbel / Michael T Madigan / Yukihiro Kimura / Zheng-Yu Wang-Otomo /
PubMed Abstract is a moderately halophilic purple nonsulfur bacterium whose unique cell wall composition and phylogeny are distinct from those of all other purple phototrophs. Here we present a cryo-EM structure ... is a moderately halophilic purple nonsulfur bacterium whose unique cell wall composition and phylogeny are distinct from those of all other purple phototrophs. Here we present a cryo-EM structure and biochemical analysis of the light-harvesting 1-reaction center (LH1-RC) complex from at 2.29 Å resolution. The LH1 complex forms a closed ring structure with 16 αβ-polypeptides surrounding the RC and contains 16 phosphatidylglycerols regularly positioned between the β-polypeptides. Extensive interactions were observed between the C-terminal domains of LH1 α-and β-polypeptides and between the regularly arranged phosphatidylglycerols and β-polypeptides, supporting the hypothesis that LH1 C-terminal interactions define the post-translational truncation sites of αβ-polypeptides in phototrophic purple bacteria. Multiple insertions were identified in the membrane-extruded RC cytochrome- and H-subunits of . Insertions in the periplasm-exposed cytochrome subunit contain high proportions of Gly, Asp, and Glu, contributing to an overall negatively charged surface of this subunit. The cytoplasm-exposed H-subunit contained an unusually long 57-residue insert rich in Pro and Ala that was invisible in the cryo-EM density map, indicating its highly flexible nature. The extensive Pro-Ala repetitive motifs in this insertion points to a regulatory role in assemblies of the RC and LH1-RC complexes. The structural features of LH1-RC are also discussed in relation to differences in the physiological environment between the periplasmic and cytoplasmic sides of membranes in halophiles, necessary for maintaining cellular activities under the high ionic strength conditions of hypersaline environments.
External linksBiochemistry / PubMed:40551662
MethodsEM (single particle)
Resolution2.3 Å
Structure data

63714

9m8m

EMDB-63714, PDB-9m8m:
Structure of photosynthetic LH1-RC complex the Halophilic Nonsulfur Purple Bacterium, Rhodothalassium salexigens
Method: EM (single particle) / Resolution: 2.3 Å

EMDB-64946: Map including micelle density from the photosynthetic LH1-RC complex of the halophilic nonsulfur purple bacterium Rhodothalassium salexigens
Method: EM (single particle) / Resolution: 2.3 Å

Chemicals

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-HEC:
HEME C

ChemComp-Z41:
(2S)-3-hydroxypropane-1,2-diyl dihexadecanoate

ChemComp-PLM:
PALMITIC ACID

ChemComp-MG:
Unknown entry

ChemComp-CA:
Unknown entry

ChemComp-BCL:
BACTERIOCHLOROPHYLL A

ChemComp-BPH:
BACTERIOPHEOPHYTIN A

ChemComp-U10:
UBIQUINONE-10

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

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

ChemComp-FE:
Unknown entry

PDB-1l8q:
CRYSTAL STRUCTURE OF DNA REPLICATION INITIATION FACTOR

ChemComp-CRT:
SPIRILLOXANTHIN

ChemComp-HOH:
WATER

Source
  • rhodothalassium salexigens dsm 2132 (bacteria)
KeywordsPHOTOSYNTHESIS / LH1-RC COMPLEX / PURPLE BACTERIA

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