Two-dimensional crystallization and electron crystallography of MAPEG proteins.
Members of the membrane-associated proteins in the eicosanoid and glutathione metabolism (MAPEG) superfamily have been subjected to two-dimensional crystallization experiments. A common denominator for successful attempts has been the use of a low lipid/protein ratio in the range of 1-9 (mol/mol). Electron crystallography demonstrated either hexagonal or orthorhombic packing of trimeric protein units. Three-dimensional structure analysis of the MAPEG member microsomal glutathione transferase 1 has shown that the monomer for this protein contains a left-handed bundle of four transmembrane helices. It is likely that this is a common structural motif for MAPEG proteins, because projection maps of all structurally characterized members are very similar.
Hebert
Hans
H
Department of Biosciences at Novum, Karolinska Institute, Huddinge, Sweden.
Jegerschöld
Caroline
C
Bhakat
Priyaranjan
P
Holm
Peter J
PJ
D000818:Animals; D003460:Crystallization; D015777:Eicosanoids / Q000378:metabolism*; D005978:Glutathione / Q000378:metabolism*; D005982:Glutathione Transferase / Q000737:chemistry* / Q000378:metabolism; D007527:Isoenzymes / Q000737:chemistry* / Q000378:metabolism; D008297:Male; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism; D008862:Microsomes, Liver / Q000201:enzymology; D008958:Models, Molecular; D005810:Multigene Family; D011487:Protein Conformation; D051381:Rats; D017207:Rats, Sprague-Dawley
D015777:Eicosanoids; D007527:Isoenzymes; D008565:Membrane Proteins; D005982:Glutathione Transferase; D005978:Glutathione