X-ray crystal structure of the YM210W mutant reaction centre from Rhodobacter sphaeroides.
The X-ray crystal structure of a reaction centre from Rhodobacter sphaeroides with a mutation of tyrosine M210 to tryptophan (YM210W) has been determined to a resolution of 2.5 A. Structural conservation is very good throughout the body of the protein, with the tryptophan side chain adopting a position in the mutant complex closely resembling that of the tyrosine in the wild-type complex. The spectroscopic properties of the YM210W reaction centre are discussed with reference to the structural data, with particular focus on evidence that the introduction of the bulkier tryptophan in place of the native tyrosine may cause a small tilt of the macrocycle of the B(L) monomeric bacteriochlorophyll.
McAuley
K E
KE
Division of Biochemistry, University of Glasgow, Glasgow, UK.
Fyfe
P K
PK
Cogdell
R J
RJ
Isaacs
N W
NW
Jones
M R
MR
D045342:Light-Harvesting Protein Complexes; D008958:Models, Molecular; D009154:Mutation; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry* / Q000235:genetics; D011487:Protein Conformation; D012242:Rhodobacter sphaeroides / Q000737:chemistry* / Q000235:genetics; D014364:Tryptophan / Q000737:chemistry; D014443:Tyrosine / Q000737:chemistry; D014961:X-Ray Diffraction
D045342:Light-Harvesting Protein Complexes; D045322:Photosynthetic Reaction Center Complex Proteins; D014443:Tyrosine; D014364:Tryptophan