Document Detail

The three-dimensional structure of CsmA: a small antenna protein from the green sulfur bacterium Chlorobium tepidum.
MedLine Citation:
PMID:  18652828     Owner:  NLM     Status:  MEDLINE    
The structure of the chlorosome baseplate protein CsmA from Chlorobium tepidum in a 1:1 chloroform:methanol solution was determined using liquid-state NMR spectroscopy. The data reveal that the 59-residue protein is predominantly alpha-helical with a long helical domain extending from residues V6 to L36, containing a putative bacteriochlorophyll a binding domain, and a short helix in the C-terminal part extending from residues M41 to G49. These elements are compatible with a model of CsmA having the long N-terminal alpha-helical stretch immersed into the lipid monolayer confining the chlorosome and the short C-terminal helix protruding outwards, thus available for interaction with the Fenna-Matthews-Olson antenna protein.
Marie Østergaard Pedersen; Jarl Underhaug; Jens Dittmer; Mette Miller; Niels Chr Nielsen
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2008-07-22
Journal Detail:
Title:  FEBS letters     Volume:  582     ISSN:  0014-5793     ISO Abbreviation:  FEBS Lett.     Publication Date:  2008 Aug 
Date Detail:
Created Date:  2008-08-12     Completed Date:  2008-10-14     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0155157     Medline TA:  FEBS Lett     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  2869-74     Citation Subset:  IM    
Center for Insoluble Protein Structures (inSPIN), Interdisciplinary Nanoscience Center (iNANO) and Department of Chemistry, University of Aarhus, Langelandsgade 140, Aarhus C, Denmark.
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MeSH Terms
Bacterial Proteins / chemistry*
Chlorobium / metabolism*
Nuclear Magnetic Resonance, Biomolecular
Protein Conformation
Reg. No./Substance:
0/Bacterial Proteins; 0/CsmA protein, Chlorobium tepidum

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