Schmidt-Krey I, Murata K, Hirai T, Mitsuoka K, Cheng Y, Morgenstern R, Fujiyoshi Y, Hebert H
Center for Structural Biochemistry, Department of Biosciences, Karolinska Institutet, Huddinge, S-141 57, Sweden.
J Mol Biol. 1999 Apr 30;288(2):243-53. doi: 10.1006/jmbi.1999.2683.
The formation of two-dimensional crystals of the membrane-bound enzyme microsomal glutathione transferase is sensitive to fractional changes in the lipid-to-protein ratio. Variation of this parameter results in crystal polymorphism. The projection structure of a p6 crystal form of the enzyme has been determined by the use of electron crystallography. The unit cell at 3 A resolution is comprised of two trimers. The hexagonal p6 and the orthorhombic p21212 crystal types have common elements in the packing arrangement which imply dominant crystal contacts. An overall structural similarity between the protein molecules in the two crystal forms is suggested by the projection maps. Furthermore, a comparison of the p6 and p21212 projection maps identifies additional corresponding protein densities which could not be assigned to the microsomal glutathione transferase trimer previously. Surprisingly, an ambiguity of the rotational orientation was found for trimers interspersed at certain positions within the crystal lattice.
