Ke. Mcauley et al., X-ray crystal structure of the YM210W mutant reaction centre from Rhodobacter sphaeroides, FEBS LETTER, 467(2-3), 2000, pp. 285-290
The X-ray crystal structure of a reaction centre from Rhodobacter sphaeroid
es with a mutation of tyrosine M210 to tryptophan (YM210W) has been determi
ned to a resolution of 2.5 Angstrom. Structural conservation is very good t
hroughout 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 particula
r focus on evidence that the introduction of the bulkier tryptophan in plac
e of the native tyrosine may cause a small tilt of the macrocycle of the B-
L monomeric bacteriochlorophyll. (C) 2000 Federation of European Biochemica
l Societies.