X-ray crystallographic and solution state nuclear magnetic resonance spectroscopic investigations of NADP+ binding to ferredoxin NADP reductase from Pseudomonas aeruginosa.

ABSTRACT: The ferredoxin nicotinamide adenine dinucleotide phosphate reductase from Pseudomonas aeruginosa ( pa-FPR) in complex with NADP (+) has been characterized by X-ray crystallography and in solution by NMR spectroscopy. The structure of the complex revealed that pa-FPR harbors a preformed NADP (+) binding pocket where the cofactor binds with minimal structural perturbation of the enzyme. These findings were complemented by obtaining sequential backbone resonance assignments of this 29518 kDa enzyme, which enabled the study of the pa-FPR-NADP complex by monitoring chemical shift perturbations induced by addition of NADP (+) or the inhibitor adenine dinucleotide phosphate (ADP) to pa-FPR. The results are consistent with a preformed NADP (+) binding site and also demonstrate that the pa-FPR-NADP

SUBMITTER: Wang A 

PROVIDER: S-EPMC2792877 | biostudies-literature | 2008 Aug

REPOSITORIES: biostudies-literature