ID 56313
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Yu, Long-Jiang Research Institute for Interdisciplinary Science, Graduate School of Natural Science and Technology, Okayama University
Suga, Michihiro Research Institute for Interdisciplinary Science, Graduate School of Natural Science and Technology, Okayama University
Wang-Otomo, Zheng-Yu Faculty of Science, Ibaraki University
Shen, Jian-Ren Research Institute for Interdisciplinary Science, Graduate School of Natural Science and Technology, Okayama University
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.
Note
This is an Accepted Manuscript of an article published by Springer Nature
Published Date
2018-04-04
Publication Title
Nature
Volume
volume556
Publisher
Springer Nature
Start Page
209
End Page
213
ISSN
0028-0836
NCID
AA00752384
Content Type
Journal Article
language
英語
OAI-PMH Set
岡山大学
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isVersionOf https://doi.org/10.1038/s41586-018-0002-9