Beta-lactamase TEM1 of E. coli. Crystal structure determination at 2.5 A resolution.
The crystal structure of beta-lactamase TEM1 from E. coli has been solved to 2.5 A resolution by X-ray diffraction methods and refined to a crystallographic R-factor of 22.7%. The structure was determined by multiple isomorphous replacement using four heavy atom derivatives. The solution from molecular replacement, using a polyalanine model constructed from the C alpha coordinates of S. Aureus PCl enzyme, provided a set of phases used for heavy atom derivatives analysis. The E. coli beta-lactamase TEM1 is made up of two domains whose topology is similar to that of the PCl enzyme. However, global superposition of the two proteins shows significant differences.
Jelsch
C
C
Laboratoire de Cristallographie Biologique, IBMC du CNRS, Strasbourg, France.
Lenfant
F
F
Masson
J M
JM
Samama
J P
JP
D000595:Amino Acid Sequence; D004926:Escherichia coli / Q000201:enzymology*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D014961:X-Ray Diffraction; D001618:beta-Lactamases / Q000737:chemistry*
D001618:beta-Lactamases; C034413:beta-lactamase TEM-1