1h85

FERREDOXIN:NADP+ REDUCTASE MUTANT WITH VAL 136 REPLACED BY LEU (V136L)

spinqualitylabelsall models 1h85, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1h85 is a 1 chain structure with sequence from Anabaena pcc7119. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FAD, SO4 Related: 1que, 1b2r, 1bjk, 1e62, 1e63, 1e64, 1quf Activity: Ferredoxin--NADP(+) reductase, with EC number 1.18.1.2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed In the ferredoxin-NADP(+) reductase (FNR)/ferredoxin (Fd) system, an aromatic amino acid residue on the surface of Anabaena Fd, Phe-65, has been shown to be essential for the electron transfer (ET) reaction. We have investigated further the role of hydrophobic interactions in complex stabilization and ET between these proteins by replacing three hydrophobic residues, Leu-76, Leu-78, and Val-136, situated on the FNR surface in the vicinity of its FAD cofactor. Whereas neither the ability of FNR to accept electrons from NADPH nor its structure appears to be affected by the introduced mutations, different behaviors with Fd are observed. Thus, the ET interaction with Fd is almost completely lost upon introduction of negatively charged side chains. In contrast, only subtle changes are observed upon conservative replacement. Introduction of Ser residues produces relatively sizable alterations of the FAD redox potential, which can explain the modified behavior of these mutants. The introduction of bulky aromatic side chains appears to produce rearrangements of the side chains at the FNR/Fd interaction surface. Thus, subtle changes in the hydrophobic patch influence the rates of ET to and from Fd by altering the binding constants and the FAD redox potentials, indicating that these residues are especially important in the binding and orientation of Fd for efficient ET. These results are consistent with the structure reported for the Anabaena FNR.Fd complex. Role of a cluster of hydrophobic residues near the FAD cofactor in Anabaena PCC 7119 ferredoxin-NADP+ reductase for optimal complex formation and electron transfer to ferredoxin.,Martinez-Julvez M, Nogues I, Faro M, Hurley JK, Brodie TB, Mayoral T, Sanz-Aparicio J, Hermoso JA, Stankovich MT, Medina M, Tollin G, Gomez-Moreno C J Biol Chem. 2001 Jul 20;276(29):27498-510. Epub 2001 May 7. PMID:11342548 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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