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  Two-dimensional structure of light harvesting complex II (LHII) from the purple bacterium Rhodovulum sulfidophilum and comparison with LHII from Rhodopseudomonas acidophila

Savage, H., Cyrklaff, M., Montoya, G., Kühlbrandt, W., & Sinning, I. (1996). Two-dimensional structure of light harvesting complex II (LHII) from the purple bacterium Rhodovulum sulfidophilum and comparison with LHII from Rhodopseudomonas acidophila. Structure, 4(3), 243-252. doi:10.1016/s0969-2126(96)00029-9.

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 Creators:
Savage, Hugh1, Author
Cyrklaff, Marek1, Author
Montoya, Guillermo1, Author
Kühlbrandt, Werner1, Author                 
Sinning, Irmgard1, Author
Affiliations:
1European Molecular Biology Laboratory, 6900 Heidelberg, Germany, ou_persistent22              

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Free keywords: cryo-electron crystallography; energy transfer; LHII complex; membrane protein; two-dimensional crystallization
 Abstract: Background: Within the membranes of photosynthetic bacteria, up to three types of light harvesting complexes (LHI, LHII, LHIII) are found. These complexes absorb photons and transfer the excitation energy to the photosynthetic reaction centre. The LH complexes comprise units that contain alpha and beta polypeptides with associated pigment molecules.

Results: The structure of LHII complex from Rhodovulum sulfidophilum has been examined to a resolution of 7 A using electron microscopy. The complex is a nonamer containing nine alphabeta subunits. These are arranged in two radially symmetric concentric cylinders, with the nine alpha chains positioned in the inner cylinder and the nine beta chains forming the outer cylinder. The 18 transmembrane helices are readily observed in the projection maps, along with 18 additional peaks attributed to the pigment molecules.

Conclusions: The determination of more structures of LH complexes will uncover the full extent of the variability of the oligomerization states in different bacteria and also in the native membrane. The analysis of two-dimensional crystals allows a rapid determination of key structural features and the oligomeric state of the complex. Comparison of our structure determined by electron microscopy with the recently solved X-ray structure indicates that the results of the two methods are complementary.

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Language(s): eng - English
 Dates: 1996-01-151995-12-071996-01-192004-06-051996-03-15
 Publication Status: Issued
 Pages: 10
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/s0969-2126(96)00029-9
PMID: 8805531
 Degree: -

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Title: Structure
  Other : Structure
Source Genre: Journal
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Publ. Info: London : Cell Press
Pages: - Volume / Issue: 4 (3) Sequence Number: - Start / End Page: 243 - 252 Identifier: ISSN: 0969-2126
CoNE: https://pure.mpg.de/cone/journals/resource/954927002244_1