3LVB

Crystal structure of the Ferredoxin:NADP+ reductase from maize root at 1.7 angstroms - Test Set Withheld

Summary for 3LVB

• Entry DOI: 10.2210/pdb3lvb/pdb
• Related: 1JB9 3LO8
• Descriptor: Ferredoxin-NADP reductase, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total)
• Functional Keywords: electron transport, oxidoreductase
• Biological source: Zea mays (maize)
• Total number of polymer chains: 1
• Total formula weight: 35634.01

Authors

Faber, H.R.,Karplus, P.A.,Aliverti, A.,Ferioli, C.,Spinola, M. (deposition date: 2010-02-19, release date: 2010-03-16, Last modification date: 2024-11-20)

Primary citation

Aliverti, A.,Faber, R.,Finnerty, C.M.,Ferioli, C.,Pandini, V.,Negri, A.,Karplus, P.A.,Zanetti, G.
Biochemical and crystallographic characterization of ferredoxin-NADP(+) reductase from nonphotosynthetic tissues
Biochemistry, 40:14501-14508, 2001

PubMed Abstract: Distinct forms of ferredoxin-NADP(+) reductase are expressed in photosynthetic and nonphotosynthetic plant tissues. Both enzymes catalyze electron transfer between NADP(H) and ferredoxin; whereas in leaves the enzyme transfers reducing equivalents from photoreduced ferredoxin to NADP(+) in photosynthesis, in roots it has the opposite physiological role, reducing ferredoxin at the expense of NADPH mainly for use in nitrate assimilation. Here, structural and kinetic properties of a nonphotosynthetic isoform were analyzed to define characteristics that may be related to tissue-specific function. Compared with spinach leaf ferredoxin-NADP(+) reductase, the recombinant corn root isoform showed a slightly altered absorption spectrum, a higher pI, a >30-fold higher affinity for NADP(+), greater susceptibility to limited proteolysis, and an approximately 20 mV more positive redox potential. The 1.7 A resolution crystal structure is very similar to the structures of ferredoxin-NADP(+) reductases from photosynthetic tissues. Four distinct structural features of this root ferredoxin-NADP(+) reductases are an alternate conformation of the bound FAD molecule, an alternate path for the amino-terminal extension, a disulfide bond in the FAD-binding domain, and changes in the surface that binds ferredoxin.

PubMed: 11724563

Experimental method

X-RAY DIFFRACTION (1.7 Å)