English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Cryo-EM structure of the whole photosynthetic reaction center apparatus from the green sulfur bacterium Chlorobaculum tepidum

Xie, H., Lyratzakis, A., Khera, R., Koutantou, M., Welsch, S., Michel, H., et al. (2023). Cryo-EM structure of the whole photosynthetic reaction center apparatus from the green sulfur bacterium Chlorobaculum tepidum. Proceedings of the National Academy of Sciences of the United States of America, 120(5): e2216734120. doi:10.1073/pnas.2216734120.

Item is

Files

hide Files
:
pnas.2216734120.pdf (Any fulltext), 7MB
Name:
pnas.2216734120.pdf
Description:
-
OA-Status:
Not specified
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show

Creators

hide
 Creators:
Xie, Hao1, Author                 
Lyratzakis, Alexandros2, Author
Khera, Radhika1, Author                 
Koutantou, Myrto2, Author
Welsch, Sonja3, Author                 
Michel, Hartmut1, Author                 
Tsiotis, Georgios2, Author
Affiliations:
1Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
2Department of Chemistry, University of Crete, Voutes Heraklion GR-70013, Greece, ou_persistent22              
3Central Electron Microscopy Facility, Max Planck Institute of Biophysics, Max Planck Society, ou_3249263              

Content

hide
Free keywords: Cryo-EM; photosynthesis; reaction center; green sulfur bacterium; Chlorobaculum tepidum
 Abstract: Light energy absorption and transfer are very important processes in photosynthesis. In green sulfur bacteria light is absorbed primarily by the chlorosomes and its energy is transferred via the Fenna–Matthews–Olson (FMO) proteins to a homodimeric reaction center (RC). Here, we report the cryogenic electron microscopic structure of the intact FMO-RC apparatus from Chlorobaculum tepidum at 2.5 Å resolution. The FMO-RC apparatus presents an asymmetric architecture and contains two FMO trimers that show different interaction patterns with the RC core. Furthermore, the two permanently bound transmembrane subunits PscC, which donate electrons to the special pair, interact only with the two large PscA subunits. This structure fills an important gap in our understanding of the transfer of energy from antenna to the electron transport chain of this RC and the transfer of electrons from reduced sulfur compounds to the special pair.

Details

hide
Language(s): eng - English
 Dates: 2022-09-302022-12-272023-01-24
 Publication Status: Published online
 Pages: 11
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1073/pnas.2216734120
PMID: 36693097
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

hide
Title: Proceedings of the National Academy of Sciences of the United States of America
  Other : PNAS
  Other : Proceedings of the National Academy of Sciences of the USA
  Abbreviation : Proc. Natl. Acad. Sci. U. S. A.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Washington, D.C. : National Academy of Sciences
Pages: - Volume / Issue: 120 (5) Sequence Number: e2216734120 Start / End Page: - Identifier: ISSN: 0027-8424
CoNE: https://pure.mpg.de/cone/journals/resource/954925427230