title: A preliminary description of the crystal structure of gamma-glutamyltranspeptidase from E. coli K-12.
abstract: 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.
authors.affiliation: Department of Synchrotron Radiation Science, Graduate University for Advanced Studies and Photon Factory, National Laboratory for High Energy Physics, Ibaraki.
authors.forename: H
authors.initials: H
authors.lastname: Sakai
authors.forename: N
authors.initials: N
authors.lastname: Sakabe
authors.forename: K
authors.initials: K
authors.lastname: Sasaki
authors.forename: W
authors.initials: W
authors.lastname: Hashimoto
authors.forename: H
authors.initials: H
authors.lastname: Suzuki
authors.forename: H
authors.initials: H
authors.lastname: Tachi
authors.forename: H
authors.initials: H
authors.lastname: Kumagai
authors.forename: K
authors.initials: K
authors.lastname: Sakabe
mesh_terms: D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology*; D011487:Protein Conformation; D005723:gamma-Glutamyltransferase / Q000737:chemistry*
chemical_list: D005723:gamma-Glutamyltransferase