Crystal structure of a phosphonate monoester hydrolase from rhizobium leguminosarum: a new member of the alkaline phosphatase superfamily

A New Member of the Alkaline Phosphatase Superfamily with a Formylglycine Nucleophile: Structural and Kinetic Characterisation of a Phosphonate Monoester Hydrolase/Phosphodiesterase from Rhizobium Leguminosarum.

0.1M TRIS-HCL PH 8.5, 25% PEG 4000, 0.2M SODIUM ACETATE

MANGANESE (II) ION (MN): TYPE OF METAL ION AND OCCUPANCY
WERE ASSIGNED ON THE BASIS OF MICROPIXE DATA AND VALENCE
BOND CALCULATIONS
CALCIUM ION (CA): TYPE OF METAL ION AND OCCUPANCY WERE
ASSIGNED ON THE BASIS OF MICROPIXE DATA AND VALENCE BOND
CALCULATIONS

RESIDUES 1-29 IN THE SEQUENCE ORIGINATE FROM A STREP-TAG
AND A LINKER, THE ENZYME SEQUENCE STARTS WITH RESIDUE
MET30
RESIDUE 57 IS A CASE OF MICROHETEROGENEITY WHERE MORE
THAN ONE IDENTITY IS OBSERVED FOR A PARTICULAR RESIDUE
NUMBER. AT POSITION 57 OF THE PROTEIN CHAIN A, BOTH DDZ
AND CYS ARE PRESENT AT 0.60 AND 0.40 OCCUPANCIES
RESPECTIVELY.

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.

PHOSPHONATE MONOESTER HYDROLASE, HYDROLASE, PLASMID, FORMYLGLYCINE, PHOSPHODIESTERASE, ALKALINE PHOSPHATASE SUPERFAMILY