2CWF

Crystal Structure of delta1-piperideine-2-carboxylate reductase from Pseudomonas syringae complexed with NADPH

Summary for 2CWF

• Entry DOI: 10.2210/pdb2cwf/pdb
• Related: 2CWH
• Descriptor: delta1-piperideine-2-carboxylate reductase, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total)
• Functional Keywords: nadph dependent enzyme, oxidoreductase
• Biological source: Pseudomonas syringae pv. tomato
• Total number of polymer chains: 2
• Total formula weight: 74071.07

Authors

Goto, M.,Muramatsu, H.,Mihara, H.,Kurihara, T.,Esaki, N.,Omi, R.,Miyahara, I.,Hirotsu, K. (deposition date: 2005-06-20, release date: 2005-10-04, Last modification date: 2024-03-13)

Primary citation

Goto, M.,Muramatsu, H.,Mihara, H.,Kurihara, T.,Esaki, N.,Omi, R.,Miyahara, I.,Hirotsu, K.
Crystal structures of Delta1-piperideine-2-carboxylate/Delta1-pyrroline-2-carboxylate reductase belonging to a new family of NAD(P)H-dependent oxidoreductases: conformational change, substrate recognition, and stereochemistry of the reaction
J.Biol.Chem., 280:40875-40884, 2005

PubMed Abstract: Delta(1)-Piperideine-2-carboxylate/Delta(1)-pyrroline-2-carboxylate reductase from Pseudomonas syringae pv. tomato belongs to a novel sub-class in a large family of NAD(P)H-dependent oxidoreductases distinct from the conventional MDH/LDH superfamily characterized by the Rossmann fold. We have determined the structures of the following three forms of the enzyme: the unliganded form, the complex with NADPH, and the complex with NADPH and pyrrole-2-carboxylate at 1.55-, 1.8-, and 1.7-A resolutions, respectively. The enzyme exists as a dimer, and the subunit consists of three domains; domain I, domain II (NADPH binding domain), and domain III. The core of the NADPH binding domain consists of a seven-stranded predominantly antiparallel beta-sheet fold (which we named SESAS) that is characteristic of the new oxidoreductase family. The enzyme preference for NADPH over NADH is explained by the cofactor binding site architecture. A comparison of the overall structures revealed that the mobile domains I and III change their conformations to produce the catalytic form. This conformational change plays important roles in substrate recognition and the catalytic process. The active site structure of the catalytic form made it possible to identify the catalytic Asp:Ser:His triad and investigate the catalytic mechanism from a stereochemical point of view.

PubMed: 16192274
DOI: 10.1074/jbc.M507399200

Experimental method

X-RAY DIFFRACTION (1.8 Å)