1GAQ

CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN FERREDOXIN AND FERREDOXIN-NADP+ REDUCTASE

Summary for 1GAQ

• Entry DOI: 10.2210/pdb1gaq/pdb
• Related: 1GAW
• Descriptor: FERREDOXIN-NADP+ REDUCTASE, FERREDOXIN I, FLAVIN-ADENINE DINUCLEOTIDE, ... (5 entities in total)
• Functional Keywords: oxidoreductase/electron transport, oxidoreductase-electron transport complex
• Biological source: Zea mays; More
• Cellular location: Plastid, chloroplast: P27787
• Total number of polymer chains: 3
• Total formula weight: 82986.19

Authors

Kurisu, G.,Kusunoki, M.,Hase, T. (deposition date: 2000-05-08, release date: 2001-02-07, Last modification date: 2023-12-27)

Primary citation

Kurisu, G.,Kusunoki, M.,Katoh, E.,Yamazaki, T.,Teshima, K.,Onda, Y.,Kimata-Ariga, Y.,Hase, T.
Structure of the electron transfer complex between ferredoxin and ferredoxin-NADP(+) reductase.
Nat.Struct.Biol., 8:117-121, 2001

PubMed Abstract: All oxygenic photosynthetically derived reducing equivalents are utilized by combinations of a single multifuctional electron carrier protein, ferredoxin (Fd), and several Fd-dependent oxidoreductases. We report the first crystal structure of the complex between maize leaf Fd and Fd-NADP(+) oxidoreductase (FNR). The redox centers in the complex--the 2Fe-2S cluster of Fd and flavin adenine dinucleotide (FAD) of FNR--are in close proximity; the shortest distance is 6.0 A. The intermolecular interactions in the complex are mainly electrostatic, occurring through salt bridges, and the interface near the prosthetic groups is hydrophobic. NMR experiments on the complex in solution confirmed the FNR recognition sites on Fd that are identified in the crystal structure. Interestingly, the structures of Fd and FNR in the complex and in the free state differ in several ways. For example, in the active site of FNR, Fd binding induces the formation of a new hydrogen bond between side chains of Glu 312 and Ser 96 of FNR. We propose that this type of molecular communication not only determines the optimal orientation of the two proteins for electron transfer, but also contributes to the modulation of the enzymatic properties of FNR.

PubMed: 11175898
DOI: 10.1038/84097

Experimental method

X-RAY DIFFRACTION (2.59 Å)