2k37

Publication Abstract from PubMed

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.

The three-dimensional structure of CsmA: A small antenna protein from the green sulfur bacterium Chlorobium tepidum.,Pedersen MO, Underhaug J, Dittmer J, Miller M, Nielsen NC FEBS Lett. 2008 Aug 20;582(19):2869-74. Epub 2008 Jul 22. PMID:18652828^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.