Crystal structure of the Delta-pyrroline-5-carboxylate dehydrogenase from Mycobacterium tuberculosis bound with NAD

Characterization of the proline-utilization pathway in Mycobacterium tuberculosis through structural and functional studies.

Delta-1-pyrroline-5-carboxylate dehydrogenase

PROBABLE PYRROLINE-5-CARBOXYLATE DEHYDROGENASE ROCA

0.1 M Bicine/Tris pH 8.1, 12% polyethylene glycol (PEG) 1000, 12% PEG 3350, 12% 2-methyl-2,4-pentandiol (MPD), 0.03 M sodium nitrate, 0.03 M disodium hydrogen phosphate and 0.03 M ammonium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 291K

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. STRUCTURE CONSISTS IN AN ARRANGEMENT OF ORDERED AND DISORDERED LAYERS RESULTING IN GAPS BETWEEN ORDERED MOLECULES. ALTHOUGH NO MOLECULES ARE MODELLED WITHIN THIS EMPTY LAYER, MAD DATA FROM SEMET-PRUA CRYSTALS INDICATES THAT PROTEIN ELECTRON DENSITY EXISTS WITHING THESE GAPS AND SUGGESTS A MOTION OF THE ENTIRE LAYER.

Delta-1-pyrroline-5-carboxylate dehydrogenase (E.C.1.5.1.12)

Rossmann fold, pyrroline-5-carboxylate dehtdrogenase, pyrroline-5-carboxylic acid, dehydrogenation, OXIDOREDUCTASE