Crystallization and X-ray diffraction study of the Streptomyces K15 penicillin-binding DD-transpeptidase.
The 262 amino acid residue long DD-transpeptidase/penicillin-binding protein of Streptomyces K15 has been crystallized at room temperature by using the hanging drop vapour diffusion technique. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit cell parameters a = 46.4 A, b = 54.1 A and c = 108.3 A. They contain one protein molecule per asymmetric unit and diffract to about 1.9 A. X-ray data have been collected to 2.0 A from a native crystal. The previously published amino acid sequence of the protein has been corrected at positions 71, 72, 113, 114 and 156.
Englebert
S
S
Centre d'Ingénierie des Protéines, Université de Liège, Belgium.
Charlier
P
P
Fonzé
E
E
To'th
Y
Y
Vermeire
M
M
Van Beeumen
J
J
Grandchamps
J
J
Hoffmann
K
K
Leyh-Bouille
M
M
Nguyen-Distèche
M
M
D001426:Bacterial Proteins; D002352:Carrier Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D006602:Hexosyltransferases; D013058:Mass Spectrometry; D002267:Muramoylpentapeptide Carboxypeptidase / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D046915:Penicillin-Binding Proteins; D010406:Penicillins / Q000378:metabolism*; D010458:Peptidyl Transferases; D013302:Streptomyces / Q000201:enzymology*
D001426:Bacterial Proteins; D002352:Carrier Proteins; D046915:Penicillin-Binding Proteins; D010406:Penicillins; D010458:Peptidyl Transferases; D006602:Hexosyltransferases; D002267:Muramoylpentapeptide Carboxypeptidase