Atomic model of plant light-harvesting complex by electron crystallography

Nature. 1994 Feb 17;367(6464):614-21. doi: 10.1038/367614a0.

Abstract

The structure of the light-harvesting chlorophyll a/b-protein complex, an integral membrane protein, has been determined at 3.4 A resolution by electron crystallography of two-dimensional crystals. Two of the three membrane-spanning alpha-helices are held together by ion pairs formed by charged residues that also serve as chlorophyll ligands. In the centre of the complex, chlorophyll a is in close contact with chlorophyll b for rapid energy transfer, and with two carotenoids that prevent the formation of toxic singlet oxygen.

MeSH terms

  • Amino Acid Sequence
  • Chlorophyll / chemistry
  • Conserved Sequence
  • Crystallography / methods
  • Light-Harvesting Protein Complexes
  • Lutein / chemistry
  • Membrane Proteins / chemistry
  • Microscopy, Electron
  • Models, Molecular
  • Molecular Sequence Data
  • Photosynthetic Reaction Center Complex Proteins / chemistry*
  • Protein Structure, Secondary

Substances

  • Light-Harvesting Protein Complexes
  • Membrane Proteins
  • Photosynthetic Reaction Center Complex Proteins
  • Chlorophyll
  • Lutein