title: Sequence conservation of light-harvesting and stress-response proteins in relation to the three-dimensional molecular structure of LHCII.
abstract: The structure of pea light-harvesting complex LHCII determined to 3.4 Å resolution by electron crystallography (Kühlbrandt, Wang and Fujiyoshi (1994) Nature 367: 614-621) was examined to determine the relationship between structural elements and sequence motifs conserved in the extended family of light-harvesting antennas (Chl a/b, fucoxanthin Chl a/c proteins) and membrane-intrinsic stress-induced proteins (ELIPs) to which LHCII belongs. It is predicted that the eukaryotic ELIPs can bind at least four molecules of Chl. The one-helix prokaryotic ELIP of Synechococcus was modelled as a homodimer based on the high degree of conservation of residues involved in the interactions of the first (B) and third (A) helices of LHCII.
authors.affiliation: Department of Botany, University of British Columbia, V6T 1Z4, Vancouver, B.C., Canada.
authors.forename: B R
authors.initials: BR
authors.lastname: Green
authors.forename: W
authors.initials: W
authors.lastname: Kühlbrandt