Proteins, chlorophylls and lipids: X-ray analysis of a three-way relationship.
Photosynthetic reaction centres and light harvesting complexes have been at the forefront of crystallographic studies of integral membrane proteins. In recent years, there have been spectacular advances in our understanding of the structure of (bacterio)chlorophyll-containing membrane proteins from oxygenic and anoxygenic phototrophs. In these complex structures, the protein scaffold encases different combinations of cofactors and interacts with several tightly bound lipid species that play a variety of hitherto unrecognized structural roles. Some of these lipids have relevance to the physiological function of the protein, whereas others are important for the formation of highly ordered crystals. The first site-directed mutagenesis studies of individual lipid binding sites have now underlined the importance of the lipid component for the structural stability of protein-cofactor-lipid complexes.
Fyfe
Paul K
PK
Department of Biochemistry, School of Medical Sciences, University of Bristol, University Walk, Bristol, UK BS8 1TD.
Hughes
Arwel V
AV
Heathcote
Peter
P
Jones
Michael R
MR
D001426:Bacterial Proteins / Q000737:chemistry / Q000502:physiology; D002734:Chlorophyll / Q000737:chemistry / Q000502:physiology*; D018360:Crystallography, X-Ray; D045342:Light-Harvesting Protein Complexes / Q000737:chemistry / Q000502:physiology; D008055:Lipids / Q000737:chemistry / Q000502:physiology*; D008958:Models, Molecular; D045331:Photosystem I Protein Complex / Q000737:chemistry / Q000235:genetics / Q000502:physiology; D010940:Plant Proteins / Q000737:chemistry / Q000502:physiology*; D011487:Protein Conformation
D001426:Bacterial Proteins; D045342:Light-Harvesting Protein Complexes; D008055:Lipids; D045331:Photosystem I Protein Complex; D010940:Plant Proteins; D002734:Chlorophyll