| Autor: |
Pedersen, Marie Østergaard, Underhaug, Jarl, Dittmer, Jens, Miller, Mette, Nielsen, Niels Chr. |
| Předmět: |
|
| Zdroj: |
FEBS Letters; Aug2008, Vol. 582 Issue 19, p2869-2874, 6p |
| Abstrakt: |
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 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. [Copyright &y& Elsevier] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
|
Plný text