Cryo-EM structure of the Blastochloris viridis LH1–RC complex at 2.9 Å

Pu Qian (), C. Alistair Siebert, Peiyi Wang, Daniel P. Canniffe and C. Neil Hunter ()
Additional contact information
Pu Qian: University of Sheffield
C. Alistair Siebert: Diamond Light Source
Peiyi Wang: University of Leeds
Daniel P. Canniffe: University of Sheffield
C. Neil Hunter: University of Sheffield

Nature, 2018, vol. 556, issue 7700, 203-208

Abstract: Abstract The light-harvesting 1–reaction centre (LH1–RC) complex is a key functional component of bacterial photosynthesis. Here we present a 2.9 Å 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 β-polypeptides sandwiched between 17 α- and 16 γ-polypeptides. Tight packing of the γ-apoproteins between β-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 γ-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.

Date: 2018
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DOI: 10.1038/s41586-018-0014-5

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