A preliminary description of the crystal structure of gamma-glutamyltranspeptidase from E. coli K-12.
The structure of GGT [EC 2.3.2.2] from E. coli K-12 was studied at 3 A resolution by X-ray crystallography. Initial protein phases were calculated using two kinds of Pb2+ derivatives. The phases were refined by non-crystallographic 2-fold symmetry electron density averaging combined with solvent flattening and histogram matching. The GGT molecule has overall dimensions of 60 x 50 x 40 A. There are two antiparallel beta-pleated sheets consisting of 6 and 7 beta-strands. The two beta-sheets form a wall-like structure. Twelve short alpha-helices were detected, of which the maximum length appears to be four helix turns.
Sakai
H
H
Department of Synchrotron Radiation Science, Graduate University for Advanced Studies and Photon Factory, National Laboratory for High Energy Physics, Ibaraki.
Sakabe
N
N
Sasaki
K
K
Hashimoto
W
W
Suzuki
H
H
Tachi
H
H
Kumagai
H
H
Sakabe
K
K
D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology*; D011487:Protein Conformation; D005723:gamma-Glutamyltransferase / Q000737:chemistry*
D005723:gamma-Glutamyltransferase