1qg0
From Proteopedia
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|PDB= 1qg0 |SIZE=350|CAPTION= <scene name='initialview01'>1qg0</scene>, resolution 2.5Å | |PDB= 1qg0 |SIZE=350|CAPTION= <scene name='initialview01'>1qg0</scene>, resolution 2.5Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE DINUCLEOTIDE'>FAD</scene> | + | |LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Ferredoxin--NADP(+)_reductase Ferredoxin--NADP(+) reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.18.1.2 1.18.1.2] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Ferredoxin--NADP(+)_reductase Ferredoxin--NADP(+) reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.18.1.2 1.18.1.2] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qg0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qg0 OCA], [http://www.ebi.ac.uk/pdbsum/1qg0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qg0 RCSB]</span> | ||
}} | }} | ||
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[[Category: Ottado, J.]] | [[Category: Ottado, J.]] | ||
[[Category: Zanetti, G.]] | [[Category: Zanetti, G.]] | ||
| - | [[Category: FAD]] | ||
[[Category: electron transfer]] | [[Category: electron transfer]] | ||
[[Category: flavoenzyme]] | [[Category: flavoenzyme]] | ||
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[[Category: photosynthesis]] | [[Category: photosynthesis]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:12:59 2008'' |
Revision as of 20:13, 30 March 2008
| |||||||
| , resolution 2.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Ferredoxin--NADP(+) reductase, with EC number 1.18.1.2 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
WILD-TYPE PEA FNR
Overview
The flavoenzyme ferredoxin-NADP+ reductase (FNR) catalyzes the production of NADPH during photosynthesis. Whereas the structures of FNRs from spinach leaf and a cyanobacterium as well as many of their homologs have been solved, none of these studies has yielded a productive geometry of the flavin-nicotinamide interaction. Here, we show that this failure occurs because nicotinamide binding to wild type FNR involves the energetically unfavorable displacement of the C-terminal Tyr side chain. We used mutants of this residue (Tyr 308) of pea FNR to obtain the structures of productive NADP+ and NADPH complexes. These structures reveal a unique NADP+ binding mode in which the nicotinamide ring is not parallel to the flavin isoalloxazine ring, but lies against it at an angle of approximately 30 degrees, with the C4 atom 3 A from the flavin N5 atom.
About this Structure
1QG0 is a Single protein structure of sequence from Pisum sativum. Full crystallographic information is available from OCA.
Reference
A productive NADP+ binding mode of ferredoxin-NADP + reductase revealed by protein engineering and crystallographic studies., Deng Z, Aliverti A, Zanetti G, Arakaki AK, Ottado J, Orellano EG, Calcaterra NB, Ceccarelli EA, Carrillo N, Karplus PA, Nat Struct Biol. 1999 Sep;6(9):847-53. PMID:10467097
Page seeded by OCA on Sun Mar 30 23:12:59 2008
