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Structure paper

TitleA Native LH1-RC-HiPIP Supercomplex from an Extremophilic Phototroph.
Journal, issue, pagesCommun Biol, Vol. 8, Issue 1, Page 42, Year 2025
Publish dateJan 11, 2025
AuthorsKazutoshi Tani / Ryo Kanno / Kenji V P Nagashima / Mai Kawakami / Naho Hiwatashi / Kazuna Nakata / Sakiko Nagashima / Kazuhito Inoue / Shinichi Takaichi / Endang R Purba / Malgorzata Hall / Long-Jiang Yu / Michael T Madigan / Akira Mizoguchi / Bruno M Humbel / Yukihiro Kimura / Zheng-Yu Wang-Otomo /
PubMed AbstractHalorhodospira (Hlr.) halophila strain BN9622 is an extremely halophilic and alkaliphilic purple phototrophic bacterium and has been widely used as a model for exploring the osmoadaptive and ...Halorhodospira (Hlr.) halophila strain BN9622 is an extremely halophilic and alkaliphilic purple phototrophic bacterium and has been widely used as a model for exploring the osmoadaptive and photosynthetic strategies employed by phototrophic extreme halophiles that enable them to thrive in hypersaline environments. Here we present the cryo-EM structures of (1) a unique native Hlr. halophila triple-complex formed from light-harvesting (LH1), the reaction center (RC), and high-potential iron-sulfur protein (HiPIP) at 2.44 Å resolution, and (2) a HiPIP-free LH1-RC complex at 2.64 Å resolution. Differing from the LH1 in the Hlr. halophila LH1-LH2 co-complex where LH1 encircles LH2, the RC-associated LH1 complex consists of 16 (rather than 18) αβ-subunits circularly surrounding the RC. These distinct forms of LH1 indicate that the number of subunits in a Hlr. halophila LH1 complex is flexible and its size is a function of the photocomplex it encircles. Like LH1 in the LH1-LH2 co-complex, the RC-associated LH1 complex also contained two forms of αβ-polypeptides and both dimeric and monomeric molecules of bacteriochlorophyll a. The majority of the isolated Hlr. halophila LH1-RC complexes contained the electron donor HiPIP bound to the surface of the RC cytochrome subunit near the heme-1 group. The bound HiPIP consisted of an N-terminal functional domain and a long C-terminal extension firmly attached to the cytochrome subunit. Despite overall highly negative surface-charge distributions for both the cytochrome subunit and HiPIP, the interface between the two proteins was relatively uncharged and neutral, forming a pathway for electron tunneling. The structure of the Hlr. halophila LH1-RC-HiPIP complex provides insights into the mechanism of light energy acquisition coupled with a long-distance electron donating process toward the charge separation site in a multi-extremophilic phototroph.
External linksCommun Biol / PubMed:39799244 / PubMed Central
MethodsEM (single particle)
Resolution2.4 - 2.6 Å
Structure data

39836

8z82

EMDB-39836, PDB-8z82:
Photosynthetic LH1-RC-HiPIP complex from the purple bacterium Halorhodospira halophila
Method: EM (single particle) / Resolution: 2.4 Å

39837

8z83

EMDB-39837, PDB-8z83:
Photosynthetic LH1-RC complex from the purple bacterium Halorhodospira halophila
Method: EM (single particle) / Resolution: 2.6 Å

Chemicals

ChemComp-HEC:
HEME C

ChemComp-MG:
Unknown entry


ChemComp, No image

ChemComp-LJQ:
Unknown entry

ChemComp-PLM:
PALMITIC ACID

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

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

ChemComp-BCL:
BACTERIOCHLOROPHYLL A

ChemComp-BPH:
BACTERIOPHEOPHYTIN A

ChemComp-UQ8:
Ubiquinone-8

ChemComp-FE:
Unknown entry

ChemComp-CDL:
CARDIOLIPIN / phospholipid*YM

ChemComp-MQ8:
MENAQUINONE 8

ChemComp-CRT:
SPIRILLOXANTHIN

ChemComp-SF4:
IRON/SULFUR CLUSTER

ChemComp-HOH:
WATER

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

Source
  • halorhodospira halophila (bacteria)
KeywordsPHOTOSYNTHESIS / LH1-RC

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