Purification, crystallization and preliminary X-ray analysis of the peptidoglycan N-acetylglucosamine deacetylase BC1960 from Bacillus cereus in the presence of its substrate (GlcNAc)6.
The peptidoglycan N-acetylglucosamine (GlcNAc) deacetylase BC1960 from Bacillus cereus (EC 3.5.1.33), an enzyme consisting of 275 amino acids, was crystallized in the presence of its substrate (GlcNAc)(6). The crystals belonged to the tetragonal space group P4(1)2(1)2, with unit-cell parameters a = b = 92.7, c = 242.9 A and four molecules in the asymmetric unit. A complete data set was collected at 100 K to a resolution of 2.38 A using synchrotron radiation.
Tsalafouta
Aleka
A
Department of Biology, University of Crete, PO Box 2208, GR-71110, Heraklion, Crete, Greece.
Psylinakis
Emmanuel
E
Kapetaniou
Evangelia G
EG
Kotsifaki
Dina
D
Deli
Alexandra
A
Roidis
Alexandros
A
Bouriotis
Vasilis
V
Kokkinidis
Michael
M
D000117:Acetylglucosamine / Q000737:chemistry* / Q000378:metabolism*; D000581:Amidohydrolases / Q000097:blood* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D001409:Bacillus cereus / Q000201:enzymology* / Q000235:genetics; D003460:Crystallization; D018360:Crystallography, X-Ray; D013379:Substrate Specificity
D000581:Amidohydrolases; C023079:N-acetylglucosamine deacetylase; D000117:Acetylglucosamine