1jb9

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Revision as of 21:16, 24 November 2007


1jb9, resolution 1.7Å

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Crystal Structure of The Ferredoxin:NADP+ Reductase From Maize Root AT 1.7 Angstroms

Overview

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.

About this Structure

1JB9 is a Single protein structure of sequence from Zea mays with FAD as ligand. Active as Ferredoxin--NADP(+) reductase, with EC number 1.18.1.2 Full crystallographic information is available from OCA.

Reference

Biochemical and crystallographic characterization of ferredoxin-NADP(+) reductase from nonphotosynthetic tissues., Aliverti A, Faber R, Finnerty CM, Ferioli C, Pandini V, Negri A, Karplus PA, Zanetti G, Biochemistry. 2001 Dec 4;40(48):14501-8. PMID:11724563

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