Expression, purification and preliminary X-ray crystallographic analysis of UDP-galactopyranose mutase from Deinococcus radiodurans.
UDP-galactopyranose mutase (UGM) catalyzes the interconversion of UDP-galactopyranose and UDP-galactofuranose. A UGM-substrate complex from Deinococccus radiodurans has been expressed, purified and crystallized. Crystals were obtained by the microbatch-under-oil method at room temperature. The crystals diffracted to 2.36 A resolution at the Canadian Light Source. The space group was found to be P2(1)2(1)2(1), with unit-cell parameters a = 134.0, b = 176.6, c = 221.6 A. The initial structure solution was determined by molecular replacement using UGM from Mycobacterium tuberculosis (PDB code 1v0j) as a template model.
Karunan Partha
Sarathy
S
Department of Chemistry, University of Saskatchewan, Saskatoon, Saskatchewan S7N 5C9, Canada.
Bonderoff
Sara A
SA
van Straaten
Karin E
KE
Sanders
David A R
DA
D001483:Base Sequence; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray; D017931:DNA Primers; D034301:Deinococcus / Q000201:enzymology*; D019751:Intramolecular Transferases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D011487:Protein Conformation
D017931:DNA Primers; D019751:Intramolecular Transferases; C098051:UDP-galactopyranose mutase