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

@article{Pedersen2008TheTS,
  title={The three-dimensional structure of CsmA: a small antenna protein from the green sulfur bacterium Chlorobium tepidum.},
  author={Marie \Ostergaard Pedersen and Jarl Underhaug and Jens Dittmer and Mette Miller and N. C. Nielsen},
  journal={FEBS letters},
  year={2008},
  volume={582 19},
  pages={2869-74}
}
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… CONTINUE READING

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  • G. Bodenhausen, D. J. Ruben
  • Chem. Phys. Lett
  • 1980
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