XYLOSE ISOMERASE FROM BACILLUS STEAROTHERMOPHILUS

Crystal Structures of Class II Xylose Isomerases from Two Thermophiles and a Hyperthermophile

High Level Expression of a Thermostable Bacillus Xylose (Glucose) Isomerase in Escherichia Coli

PYFDNISTIAYEGPASKNPLAFKFYNPEEKVGDKTMEEHLRFSVAYWHTFTGDGSDPFGAGNMIRPWNKYSGMDLAKARV
EAAFEFFEKLNIPFFCFHDVDIAPEGETLKETYKNLDIIVDMIEEYMKTSKTKLLWNTANLFTHPRFVHGAATSCNADVF
AYAAAKVKKGLEIAKRLGAENYVFWGGREGYETLLNTDMKLELDNLARFLHMAVDYAKEIGFDGQFLIEPKPKEPTKHQY
DFDVATALAFLQTYGLKDYFKFNIEANHATLAGHTFEHELRVARIHGMLGSVDANQGDMLLGWDTDEFPTDLYSTTLAMY
EILKNGGLGRGGLNFDAKVRRGSFEPEDLFYAHIAGMDSFAVGLKVAHRLIEDRVFDEFIEERYKSYTEGIGREIVEGTA
DFHKLEAHALQLGEIQNQSGRQERLKTLLNQYLLEVCAAR

VAPOR DIFFUSION FROM HANGING DROPS (18 DEG C): PROTEIN (A280 22) WAS IN 50 MM TRIS, 10 MM MNCL2, PH 7.5; RESERVOIR SOLUTION WAS 10% PEG, 100 MM LICL, 100 MM MES, PH 6.3; DROPS WERE FORMED FROM EQUAL PARTS OF PROTEIN AND RESERVOIR SOLUTIONS., pH 6.5, vapor diffusion - hanging drop

OCCUPANCIES OF THE MN CATIONS AND WATER HOH 501 WERE REFINED, SIMULTANEOUSLY WITH TEMPERATURE FACTORS FOR ALL ATOMS, USING THE GROUP B COMMAND IN X-PLOR. THESE OCCUPANCIES WERE THEN FIXED AT ROUNDED VALUES FOR THE SUBSEQUENT REFINEMENT PROTOCOL. DISORDERED SIDE CHAINS WERE NOT INCLUDED IN REFINEMENT.

KETOLISOMERASE, XYLOSE METABOLISM, GLUCOSE-FRUCTOSE INTERCONVERSION, HYDRIDE TRANSFER, ALPHA-BETA BARREL, METALLOENZYME, THERMOPHILE

MPYFDNISTIAYEGPASKNPLAFKFYNPEEKVGDKTMEEHLRFSVAYWHTFTGDGSDPFGAGNMIRPWNKYSGMDLAKAR
VEAAFEFFEKLNIPFFCFHDVDIAPEGETLKETYKNLDIIVDMIEEYMKTSKTKLLWNTANLFTHPRFVHGAATSCNADV
FAYAAAKVKKGLEIAKRLGAENYVFWGGREGYETLLNTDMKLELDNLARFLHMAVDYAKEIGFDGQFLIEPKPKEPTKHQ
YDFDVATALAFLQTYGLKDYFKFNIEANHATLAGHTFEHELRVARIHGMLGSVDANQGDMLLGWDTDEFPTDLYSTTLAM
YEILKNGGLGRGGLNFDAKVRRGSFEPEDLFYAHIAGMDSFAVGLKVAHRLIEDRVFDEFIEERYKSYTEGIGREIVEGT
ADFHKLEAHALQLGEIQNQSGRQERLKTLLNQYLLEVCAAR