1FNC
REFINED CRYSTAL STRUCTURE OF SPINACH FERREDOXIN REDUCTASE AT 1.7 ANGSTROMS RESOLUTION: OXIDIZED, REDUCED, AND 2'-PHOSPHO-5'-AMP BOUND STATES
Summary for 1FNC
| Entry DOI | 10.2210/pdb1fnc/pdb |
| Descriptor | FERREDOXIN-NADP+ REDUCTASE, SULFATE ION, DIHYDROFLAVINE-ADENINE DINUCLEOTIDE, ... (5 entities in total) |
| Functional Keywords | oxidoreductase (nadp+(a), ferredoxin(a)) |
| Biological source | Spinacia oleracea (spinach) |
| Cellular location | Plastid, chloroplast stroma: P00455 |
| Total number of polymer chains | 1 |
| Total formula weight | 36692.53 |
| Authors | Bruns, C.M.,Karplus, P.A. (deposition date: 1995-01-05, release date: 1995-04-20, Last modification date: 2024-02-07) |
| Primary citation | Bruns, C.M.,Karplus, P.A. Refined crystal structure of spinach ferredoxin reductase at 1.7 A resolution: oxidized, reduced and 2'-phospho-5'-AMP bound states. J.Mol.Biol., 247:125-145, 1995 Cited by PubMed Abstract: The crystal structure of spinach ferredoxin-NADP(+)-oxidoreductase (FNR), determined by multiple isomorphous replacement at 2.6 A resolution, has been refined at 1.7 A resolution to an R-factor of 17.9%. The structure of FNR bound to the competitive inhibitor 2'-phospho-5'-AMP (P-AMP) has also been refined at 1.7 A to an R-factor of 17.4% and dithionite-reduced/P-AMP-bound FNR has been refined at 2.0 A to an R-factor of 14.9%. The P-AMP-bound structure was used to construct a model for the binding of NADP+. Over 200 solvation sites were included in each structure, and many of the best defined solvation sites stabilize buried turns. A bulk solvent correction obviated the need for a low-resolution data cutoff. An acidic side-chain likely to be responsible for the low pH requirement for crystallization has been identified. Three large networks of the hydrophobic side-chains help define the FNR structure. One of these contains a large cavity far from the active site, which coincides with the lone site of sequence heterogeneity in FNR, and may provide a site for membrane attachment. The reduced structure shows that Ser96 moves toward atom N-5 of FAD and a water molecule moves toward atom N-1 of FAD, while the flavin moiety remains planar. Possible sources of a proton that must be picked up upon reduction are discussed. PubMed: 7897656DOI: 10.1006/jmbi.1994.0127 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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