Document Detail

Structure of the dimeric RC-LH1-PufX complex from Rhodobaca bogoriensis investigated by electron microscopy.
MedLine Citation:
PMID:  23148268     Owner:  NLM     Status:  MEDLINE    
Electron microscopy and single-particle averaging were performed on isolated reaction centre (RC)-antenna complexes (RC-LH1-PufX complexes) of Rhodobaca bogoriensis strain LBB1, with the aim of establishing the LH1 antenna conformation, and, in particular, the structural role of the PufX protein. Projection maps of dimeric complexes were obtained at 13 Å resolution and show the positions of the 2 × 14 LH1 α- and β-subunits. This new dimeric complex displays two open, C-shaped LH1 aggregates of 13 αβ polypeptides partially surrounding the RCs plus two LH1 units forming the dimer interface in the centre. Between the interface and the two half rings are two openings on each side. Next to the openings, there are four additional densities present per dimer, considered to be occupied by four copies of PufX. The position of the RC in our model was verified by comparison with RC-LH1-PufX complexes in membranes. Our model differs from previously proposed configurations for Rhodobacter species in which the LH1 ribbon is continuous in the shape of an S, and the stoichiometry is of one PufX per RC.
Dmitry A Semchonok; Jean-Paul Chauvin; Raoul N Frese; Colette Jungas; Egbert J Boekema
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Philosophical transactions of the Royal Society of London. Series B, Biological sciences     Volume:  367     ISSN:  1471-2970     ISO Abbreviation:  Philos. Trans. R. Soc. Lond., B, Biol. Sci.     Publication Date:  2012 Dec 
Date Detail:
Created Date:  2012-11-13     Completed Date:  2013-04-22     Revised Date:  2014-01-10    
Medline Journal Info:
Nlm Unique ID:  7503623     Medline TA:  Philos Trans R Soc Lond B Biol Sci     Country:  England    
Other Details:
Languages:  eng     Pagination:  3412-9     Citation Subset:  IM    
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MeSH Terms
Bacterial Proteins / chemistry,  ultrastructure
Cell Membrane / chemistry
Light-Harvesting Protein Complexes / chemistry*,  ultrastructure*
Membrane Proteins / chemistry,  ultrastructure
Microscopy, Electron*
Models, Molecular
Protein Conformation
Protein Multimerization*
Proteobacteria / chemistry*
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / methods
Reg. No./Substance:
0/Bacterial Proteins; 0/Light-Harvesting Protein Complexes; 0/Membrane Proteins

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