Crystal Structure of S112A/H265A double mutant of a C-C hydrolase, BphD, from Burkholderia xenovorans LB400

The Tautomeric Half-reaction of BphD, a C-C Bond Hydrolase: KINETIC AND STRUCTURAL EVIDENCE SUPPORTING A KEY ROLE FOR HISTIDINE 265 OF THE CATALYTIC TRIAD.

2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase

MTALTESSTSKFVKINEKGFSDFNIHYNEAGNGETVIMLHGGGPGAGGWSNYYRNVGPFVDAGYRVILKDSPGFNKSDAV
VMDEQRGLVNARAVKGLMDALDIDRAHLVGNAMGGATALNFALEYPDRIGKLILMGPGGLGPSMFAPMPMEGIKLLFKLY
AEPSYETLKQMLQVFLYDQSLITEELLQGRWEAIQRQPEHLKNFLISAQKAPLSTWDVTARLGEIKAKTFITWGRDDRFV
PLDHGLKLLWNIDDARLHVFSKCGAWAQWEHADEFNRLVIDFLRHA

1.9 M sodium malonate, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 100K, temperature 293K

NPPSFA, National Project on Protein Structural and Functional Analyses

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

The biological assembly is a tetramer generated from the monomer in the asymmetric unit by the operations: x, y, z; -x+1/2, -y+1/2, z+1/2; -y, x+1/2, z+1/4; y+1/2, -x, z+3/4;

C-C bond hydrolase, HYDROLASE, Structural Genomics

MTALTESSTSKFVKINEKGFSDFNIHYNEAGNGETVIMLHGGGPGAGGWSNYYRNVGPFVDAGYRVILKDSPGFNKSDAV
VMDEQRGLVNARAVKGLMDALDIDRAHLVGNSMGGATALNFALEYPDRIGKLILMGPGGLGPSMFAPMPMEGIKLLFKLY
AEPSYETLKQMLQVFLYDQSLITEELLQGRWEAIQRQPEHLKNFLISAQKAPLSTWDVTARLGEIKAKTFITWGRDDRFV
PLDHGLKLLWNIDDARLHVFSKCGHWAQWEHADEFNRLVIDFLRHA