期刊
NATURE
卷 556, 期 7700, 页码 203-+出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/s41586-018-0014-5
关键词
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资金
- Biotechnology and Biological Sciences Research Council (BBSRC) UK [BB/M000265/1]
- European Research Council [338895]
- Sheffield University Imagine programme
- Photosynthetic Antenna Research Center (PARC), an Energy Frontier Research Center - US Department of Energy, Office of Science, Office of Basic Energy Sciences [DE-SC0001035]
- European Commission [660652]
- BBSRC [BB/M000265/1] Funding Source: UKRI
The light-harvesting 1-reaction centre (LH1-RC) complex is a key functional component of bacterial photosynthesis. Here we present a 2.9 angstrom resolution cryo-electron microscopy structure of the bacteriochlorophyll b-based LH1-RC complex from Blastochloris viridis that reveals the structural basis for absorption of infrared light and the molecular mechanism of quinone migration across the LH1 complex. The triple-ring LH1 complex comprises a circular array of 17 beta-polypeptides sandwiched between 17 alpha-and 16 gamma-polypeptides. Tight packing of the gamma-apoproteins between beta-polypeptides collectively interlocks and stabilizes the LH1 structure; this, together with the short Mg-Mg distances of bacteriochlorophyll b pairs, contributes to the large redshift of bacteriochlorophyll b absorption. The 'missing' 17th gamma-polypeptide creates a pore in the LH1 ring, and an adjacent binding pocket provides a folding template for a quinone, Q(P), which adopts a compact, export-ready conformation before passage through the pore and eventual diffusion to the cytochrome bc(1) complex.
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