title: The three-dimensional structure of CsmA: a small antenna protein from the green sulfur bacterium Chlorobium tepidum.
abstract: 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.
authors.affiliation: Center for Insoluble Protein Structures (inSPIN), Interdisciplinary Nanoscience Center (iNANO) and Department of Chemistry, University of Aarhus, Langelandsgade 140, Aarhus C, Denmark.
authors.forename: Marie Østergaard
authors.initials: MØ
authors.lastname: Pedersen
authors.forename: Jarl
authors.initials: J
authors.lastname: Underhaug
authors.forename: Jens
authors.initials: J
authors.lastname: Dittmer
authors.forename: Mette
authors.initials: M
authors.lastname: Miller
authors.forename: Niels Chr
authors.initials: NC
authors.lastname: Nielsen
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D041883:Chlorobium / Q000378:metabolism*; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation
chemical_list: D001426:Bacterial Proteins; C404706:CsmA protein, Chlorobium tepidum