Structure of photosynthetic LH1-RC supercomplex at 1.9 Å resolution

Long-Jiang Yu, Michihiro Suga, Zheng Yu Wang-Otomo, Jian-Ren Shen

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

Light-harvesting complex 1 (LH1) and the reaction centre (RC) form a membrane-protein supercomplex that performs the primary reactions of photosynthesis in purple photosynthetic bacteria. The structure of the LH1-RC complex can provide information on the arrangement of protein subunits and cofactors; however, so far it has been resolved only at a relatively low resolution. Here we report the crystal structure of the calcium-ion-bound LH1-RC supercomplex of Thermochromatium tepidum at a resolution of 1.9 Å. This atomic-resolution structure revealed several new features about the organization of protein subunits and cofactors. We describe the loop regions of RC in their intact states, the interaction of these loop regions with the LH1 subunits, the exchange route for the bound quinone QB with free quinone molecules, the transport of free quinones between the inside and outside of the LH1 ring structure, and the detailed calcium-ion-binding environment. This structure provides a solid basis for the detailed examination of the light reactions that occur during bacterial photosynthesis.

Original languageEnglish
Pages (from-to)209-213
Number of pages5
JournalNature
Volume556
Issue number7700
DOIs
Publication statusPublished - Apr 1 2018

Fingerprint

Light
Protein Subunits
Photosynthesis
Ions
Calcium
Proteobacteria
Quinones
Membrane Proteins
benzoquinone

ASJC Scopus subject areas

  • General

Cite this

Structure of photosynthetic LH1-RC supercomplex at 1.9 Å resolution. / Yu, Long-Jiang; Suga, Michihiro; Wang-Otomo, Zheng Yu; Shen, Jian-Ren.

In: Nature, Vol. 556, No. 7700, 01.04.2018, p. 209-213.

Research output: Contribution to journalArticle

Yu, Long-Jiang ; Suga, Michihiro ; Wang-Otomo, Zheng Yu ; Shen, Jian-Ren. / Structure of photosynthetic LH1-RC supercomplex at 1.9 Å resolution. In: Nature. 2018 ; Vol. 556, No. 7700. pp. 209-213.
@article{caa61fa42a684343b938fee065cc9491,
title = "Structure of photosynthetic LH1-RC supercomplex at 1.9 {\AA} resolution",
abstract = "Light-harvesting complex 1 (LH1) and the reaction centre (RC) form a membrane-protein supercomplex that performs the primary reactions of photosynthesis in purple photosynthetic bacteria. The structure of the LH1-RC complex can provide information on the arrangement of protein subunits and cofactors; however, so far it has been resolved only at a relatively low resolution. Here we report the crystal structure of the calcium-ion-bound LH1-RC supercomplex of Thermochromatium tepidum at a resolution of 1.9 {\AA}. This atomic-resolution structure revealed several new features about the organization of protein subunits and cofactors. We describe the loop regions of RC in their intact states, the interaction of these loop regions with the LH1 subunits, the exchange route for the bound quinone QB with free quinone molecules, the transport of free quinones between the inside and outside of the LH1 ring structure, and the detailed calcium-ion-binding environment. This structure provides a solid basis for the detailed examination of the light reactions that occur during bacterial photosynthesis.",
author = "Long-Jiang Yu and Michihiro Suga and Wang-Otomo, {Zheng Yu} and Jian-Ren Shen",
year = "2018",
month = "4",
day = "1",
doi = "10.1038/s41586-018-0002-9",
language = "English",
volume = "556",
pages = "209--213",
journal = "Nature",
issn = "0028-0836",
publisher = "Nature Publishing Group",
number = "7700",

}

TY - JOUR

T1 - Structure of photosynthetic LH1-RC supercomplex at 1.9 Å resolution

AU - Yu, Long-Jiang

AU - Suga, Michihiro

AU - Wang-Otomo, Zheng Yu

AU - Shen, Jian-Ren

PY - 2018/4/1

Y1 - 2018/4/1

N2 - Light-harvesting complex 1 (LH1) and the reaction centre (RC) form a membrane-protein supercomplex that performs the primary reactions of photosynthesis in purple photosynthetic bacteria. The structure of the LH1-RC complex can provide information on the arrangement of protein subunits and cofactors; however, so far it has been resolved only at a relatively low resolution. Here we report the crystal structure of the calcium-ion-bound LH1-RC supercomplex of Thermochromatium tepidum at a resolution of 1.9 Å. This atomic-resolution structure revealed several new features about the organization of protein subunits and cofactors. We describe the loop regions of RC in their intact states, the interaction of these loop regions with the LH1 subunits, the exchange route for the bound quinone QB with free quinone molecules, the transport of free quinones between the inside and outside of the LH1 ring structure, and the detailed calcium-ion-binding environment. This structure provides a solid basis for the detailed examination of the light reactions that occur during bacterial photosynthesis.

AB - Light-harvesting complex 1 (LH1) and the reaction centre (RC) form a membrane-protein supercomplex that performs the primary reactions of photosynthesis in purple photosynthetic bacteria. The structure of the LH1-RC complex can provide information on the arrangement of protein subunits and cofactors; however, so far it has been resolved only at a relatively low resolution. Here we report the crystal structure of the calcium-ion-bound LH1-RC supercomplex of Thermochromatium tepidum at a resolution of 1.9 Å. This atomic-resolution structure revealed several new features about the organization of protein subunits and cofactors. We describe the loop regions of RC in their intact states, the interaction of these loop regions with the LH1 subunits, the exchange route for the bound quinone QB with free quinone molecules, the transport of free quinones between the inside and outside of the LH1 ring structure, and the detailed calcium-ion-binding environment. This structure provides a solid basis for the detailed examination of the light reactions that occur during bacterial photosynthesis.

UR - http://www.scopus.com/inward/record.url?scp=85045274375&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85045274375&partnerID=8YFLogxK

U2 - 10.1038/s41586-018-0002-9

DO - 10.1038/s41586-018-0002-9

M3 - Article

C2 - 29618814

AN - SCOPUS:85045274375

VL - 556

SP - 209

EP - 213

JO - Nature

JF - Nature

SN - 0028-0836

IS - 7700

ER -