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Cryo-EM structure of the Blastochloris viridis LH1–RC complex at 2.9 Å
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Cryo-EM structure of the Blastochloris viridis LH1–RC complex at 2.9 Å
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Journal Article
Cryo-EM structure of the Blastochloris viridis LH1–RC complex at 2.9 Å
2018
Overview
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.
A cryo-electron microscopy structure of the light-harvesting–reaction centre (LH1–RC) complex of the photosynthetic bacterium Blastochloris viridis suggests factors that underlie the large redshift in the absorption spectrum of bacteriochlorophyll in the complex and that promote quinone–quinol translocation across the LH1 ring.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ Apoproteins - ultrastructure
/ Bacterial Proteins - chemistry
/ Bacterial Proteins - metabolism
/ Bacterial Proteins - ultrastructure
/ Bacteriochlorophylls - chemistry
/ Bacteriochlorophylls - metabolism
/ Humanities and Social Sciences
/ Hyphomicrobiaceae - chemistry
/ Light-Harvesting Protein Complexes - chemistry
/ Light-Harvesting Protein Complexes - metabolism
/ Light-Harvesting Protein Complexes - ultrastructure
/ Quinones
/ Science
