The three-dimensional structure of CsmA: A small antenna protein from the green sulfur bacterium Chlorobium tepidum

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 α-helical with a long helical domain extending from residues V6 to L36...

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Published inFEBS letters Vol. 582; no. 19; pp. 2869 - 2874
Main Authors Pedersen, Marie Østergaard, Underhaug, Jarl, Dittmer, Jens, Miller, Mette, Nielsen, Niels Chr
Format Journal Article
LanguageEnglish
Published England Elsevier B.V 20.08.2008
Subjects
Bacteria
Bacterial Proteins - chemistry
Chlorobium - metabolism
Chlorobium tepidum
Chlorosome
CsmA
Green bacterium
Nuclear magnetic resonance
Nuclear Magnetic Resonance, Biomolecular
Photosynthetic antenna
Protein Conformation
Green bacterium
Chlorosome
Nuclear magnetic resonance
CsmA
Chlorobium tepidum
Photosynthetic antenna
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Summary: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 α-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 α-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.
Bibliography:ObjectType-Article-1
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ISSN:0014-5793
1873-3468
DOI:10.1016/j.febslet.2008.07.020