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TitleMolecular structure and characterization of the Thermochromatium tepidum light-harvesting 1 photocomplex produced in a foreign host.
Journal, issue, pagesBiochim Biophys Acta Bioenerg, Vol. 1865, Issue 3, Page 149050, Year 2024
Publish dateAug 1, 2024
AuthorsYi-Hao Yan / Guang-Lei Wang / Xing-Yu Yue / Fei Ma / Michael T Madigan / Zheng-Yu Wang-Otomo / Mei-Juan Zou / Long-Jiang Yu /
PubMed AbstractPurple phototrophic bacteria possess light-harvesting 1 and reaction center (LH1-RC) core complexes that play a key role in converting solar energy to chemical energy. High-resolution structures of ...Purple phototrophic bacteria possess light-harvesting 1 and reaction center (LH1-RC) core complexes that play a key role in converting solar energy to chemical energy. High-resolution structures of LH1-RC and RC complexes have been intensively studied and have yielded critical insight into the architecture and interactions of their proteins, pigments, and cofactors. Nevertheless, a detailed picture of the structure and assembly of LH1-only complexes is lacking due to the intimate association between LH1 and the RC. To study the intrinsic properties and structure of an LH1-only complex, a genetic system was constructed to express the Thermochromatium (Tch.) tepidum LH1 complex heterologously in a modified Rhodospirillum rubrum mutant strain. The heterologously expressed Tch. tepidum LH1 complex was isolated in a pure form free of the RC and exhibited the characteristic absorption properties of Tch. tepidum. Cryo-EM structures of the LH1-only complexes revealed a closed circular ring consisting of either 14 or 15 αβ-subunits, making it the smallest completely closed LH1 complex discovered thus far. Surprisingly, the Tch. tepidum LH1-only complex displayed even higher thermostability than that of the native LH1-RC complex. These results reveal previously unsuspected plasticity of the LH1 complex, provide new insights into the structure and assembly of the LH1-RC complex, and show how molecular genetics can be exploited to study membrane proteins from phototrophic organisms whose genetic manipulation is not yet possible.
External linksBiochim Biophys Acta Bioenerg / PubMed:38806091
MethodsEM (single particle)
Resolution3.11 - 3.32 Å
Structure data

36151

8jc8

EMDB-36151, PDB-8jc8:
Cryo-EM structure of the LH1 complex from thermochromatium tepidum
Method: EM (single particle) / Resolution: 3.11 Å

36154

8jc9

EMDB-36154, PDB-8jc9:
Cryo-EM structure of the LH1 complex from thermochromatium tepidum
Method: EM (single particle) / Resolution: 3.32 Å

Chemicals

ChemComp-BCL:
BACTERIOCHLOROPHYLL A

ChemComp-8K6:
Octadecane

ChemComp-CA:
Unknown entry

ChemComp-CRT:
SPIRILLOXANTHIN

ChemComp-D12:
DODECANE

Source
  • thermochromatium tepidum (bacteria)
KeywordsPHOTOSYNTHESIS / LH1 COMPLEX

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