Structure of proline utilization A with L-proline bound in the L-glutamate-gamma-semialdehyde dehydrogenase active site

1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE

Structural analysis of prolines and hydroxyprolines binding to the l-glutamate-gamma-semialdehyde dehydrogenase active site of bifunctional proline utilization A.

Crystallization experiments were set up with SmPutA (6 mg/mL) and NADH (10 mM) in a buffer containing 50 mM Tris (pH 8.0), 50 mM NaCl, 5% (w/v) glycerol, and 0.5 mM Tris(2-caboxyethyl)phosphine. Crystals were grown using a reservoir solution containing 19% PEG-3350, 0.2 M ammonium sulfate, 0.1 M magnesium chloride, 0.1 M HEPES (pH 8.0), and 0.1 M sodium formate. Cryobuffer: reservoir supplemented with 15 % PEG-200 and 50 mM L-proline

National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)

Bifunctional protein PutA (E.C.1.5.5.2,1.2.1.88)
FLAVOENZYME, ROSSMANN FOLD, PROLINE DEHYDROGNEASE, ALDEHYDE DEHYDROGENASE, PROLINE CATABOLISM, SUBSTRATE CHANNELING, BIFUNCTIONAL ENZYME, OXIDOREDUCTASE