Structure of the LH1-RC complex from Thermochromatium tepidum at 3.0 Å

Satomi Niwa, Long Jiang Yu, Kazuki Takeda, Yu Hirano, Tomoaki Kawakami, Zheng Yu Wang-Otomo, Kunio Miki

Research output: Contribution to journalArticle

132 Citations (Scopus)

Abstract

The light-harvesting core antenna (LH1) and the reaction centre (RC) of purple photosynthetic bacteria form a supramolecular complex (LH1-RC) to use sunlight energy in a highly efficient manner. Here we report the first near-atomic structure, to our knowledge, of a LH1-RC complex, namely that of a Ca2+ -bound complex from Thermochromatium tepidum, which reveals detailed information on the arrangement and interactions of the protein subunits and the cofactors. The RC is surrounded by 16 heterodimers of the LH1 αβ-subunit that form a completely closed structure. The Ca2+ ions are located at the periplasmic side of LH1. Thirty-two bacteriochlorophyll and 16 spirilloxanthin molecules in the LH1 ring form an elliptical assembly. The geometries of the pigment assembly involved in the absorption characteristics of the bacteriochlorophyll in LH1 and excitation energy transfer among the pigments are reported. In addition, possible ubiquinone channels in the closed LH1 complex are proposed based on the atomic structure.

Original languageEnglish
Pages (from-to)228-232
Number of pages5
JournalNature
Volume508
Issue number7495
DOIs
Publication statusPublished - Apr 10 2014

ASJC Scopus subject areas

  • General

Fingerprint Dive into the research topics of 'Structure of the LH1-RC complex from Thermochromatium tepidum at 3.0 Å'. Together they form a unique fingerprint.

  • Cite this

    Niwa, S., Yu, L. J., Takeda, K., Hirano, Y., Kawakami, T., Wang-Otomo, Z. Y., & Miki, K. (2014). Structure of the LH1-RC complex from Thermochromatium tepidum at 3.0 Å. Nature, 508(7495), 228-232. https://doi.org/10.1038/nature13197