Crystallization and preliminary X-ray diffraction analysis of diaminopimelate epimerase from Escherichia coli.
Diaminopimelate (DAP) epimerase (EC 5.1.1.7) catalyzes the penultimate step of lysine biosynthesis in bacteria and plants, converting L,L-diaminopimelate to meso-diaminopimelate. Here, the cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of DAP epimerase from Escherichia coli are presented. Crystals were obtained in space group P4(1)2(1)2 and diffracted to 2.0 A resolution, with unit-cell parameters a = b = 89.4, c = 179.6 A. Molecular replacement was conducted using Bacillus anthracis DAP epimerase as a search model and showed the presence of two molecules in the asymmetric unit, with an initial R(free) of 0.456 and R(work) of 0.416.
Hor
Lilian
L
School of Chemistry, The University of Melbourne, Parkville, Victoria 3010, Australia.
Dobson
Renwick C J
RC
Dogovski
Con
C
Hutton
Craig A
CA
Perugini
Matthew A
MA
D000591:Amino Acid Isomerases / Q000737:chemistry* / Q000302:isolation & purification; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology
D000591:Amino Acid Isomerases; C042032:diaminopimelate epimerase