2bgi
From Proteopedia
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X-RAY STRUCTURE OF THE FERREDOXIN-NADP(H) REDUCTASE FROM RHODOBACTER CAPSULATUS COMPLEXED WITH THREE MOLECULES OF THE DETERGENT N-HEPTYL-BETA-D-THIOGLUCOSIDE AT 1.7 ANGSTROMS
Overview
The photosynthetic bacterium Rhodobacter capsulatus contains a ferredoxin, (flavodoxin)-NADP(H) oxidoreductase (FPR) that catalyzes electron transfer, between NADP(H) and ferredoxin or flavodoxin. The structure of the enzyme, determined by X-ray crystallography, contains two domains harboring the, FAD and NADP(H) binding sites, as is typical of the FPR structural family., The FAD molecule is in a hairpin conformation in which stacking, interactions can be established between the dimethylisoalloxazine and, adenine moieties. The midpoint redox potentials of the various transitions, undergone by R. capsulatus FPR were similar to those reported for their, counterparts involved in oxygenic photosynthesis, but its catalytic, activity is orders of magnitude lower (1-2 s(-)(1) versus 200-500 ... [(full description)]
About this Structure
2BGI is a [Single protein] structure of sequence from [Rhodobacter capsulatus] with SO4, FAD, HTG and CO2 as [ligands]. Active as [[1]], with EC number [1.18.1.2]. Full crystallographic information is available from [OCA].
Reference
The ferredoxin-NADP(H) reductase from Rhodobacter capsulatus: molecular structure and catalytic mechanism., Nogues I, Perez-Dorado I, Frago S, Bittel C, Mayhew SG, Gomez-Moreno C, Hermoso JA, Medina M, Cortez N, Carrillo N, Biochemistry. 2005 Sep 6;44(35):11730-40. PMID:16128574
Page seeded by OCA on Mon Oct 29 16:46:56 2007
Categories: Rhodobacter capsulatus | Single protein | Bittel, C. | Carrillo, N. | Cortez, N. | Frago, S. | Gomez-Moreno, C. | Hermoso, J.A. | Mayhew, S.G. | Medina, M. | Nogues, I. | Perez-Dorado, J.I. | CO2 | FAD | HTG | SO4 | Electron transfer | Ferredoxin(flavodoxin)-nadp(h) reductase | Flavoproteins | Oxidoreductase
