1frq
From Proteopedia
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| - | [[Image:1frq.gif|left|200px]] | + | [[Image:1frq.gif|left|200px]] |
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| - | '''FERREDOXIN:NADP+ OXIDOREDUCTASE (FERREDOXIN REDUCTASE) MUTANT E312A''' | + | {{Structure |
| + | |PDB= 1frq |SIZE=350|CAPTION= <scene name='initialview01'>1frq</scene>, resolution 1.95Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''FERREDOXIN:NADP+ OXIDOREDUCTASE (FERREDOXIN REDUCTASE) MUTANT E312A''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1FRQ is a [ | + | 1FRQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FRQ OCA]. |
==Reference== | ==Reference== | ||
| - | Probing the function of the invariant glutamyl residue 312 in spinach ferredoxin-NADP+ reductase., Aliverti A, Deng Z, Ravasi D, Piubelli L, Karplus PA, Zanetti G, J Biol Chem. 1998 Dec 18;273(51):34008-15. PMID:[http:// | + | Probing the function of the invariant glutamyl residue 312 in spinach ferredoxin-NADP+ reductase., Aliverti A, Deng Z, Ravasi D, Piubelli L, Karplus PA, Zanetti G, J Biol Chem. 1998 Dec 18;273(51):34008-15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9852055 9852055] |
[[Category: Ferredoxin--NADP(+) reductase]] | [[Category: Ferredoxin--NADP(+) reductase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: flavoprotein]] | [[Category: flavoprotein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:13:05 2008'' |
Revision as of 09:13, 20 March 2008
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| , resolution 1.95Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , and | ||||||
| Activity: | Ferredoxin--NADP(+) reductase, with EC number 1.18.1.2 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
FERREDOXIN:NADP+ OXIDOREDUCTASE (FERREDOXIN REDUCTASE) MUTANT E312A
Overview
Ferredoxin-NADP+ reductase, the prototype of a large family of structurally related flavoenzymes, pairs single electrons carried by ferredoxin I and transfers them as a hydride to NADP+. Four mutants of the enzyme, in which Glu-312 was replaced with Asp, Gln, Leu, and Ala to probe the role of the residue charge, size, and polarity in the enzyme activity, have been heterologously expressed, purified, and characterized through steady-state, rapid kinetic studies, ligand-binding experiments, and three-dimensional structure determination by x-ray crystallography. The E312L mutant was the only one that was almost inactive (approximately 1%), whereas unexpectedly the E312A reductase was 10-100% active with the various acceptors tested. Rapid kinetic absorption spectroscopy studies demonstrated that flavin reduction by NADPH was impaired in the mutants. Furthermore, NADP(H) binding was partially perturbed. These functional and structural studies lead us to conclude that Glu-312 does not fulfil the role of proton donor during catalysis, but it is required for proper binding of the nicotinamide ring of NADP(H). In addition, its charge modulates the two one-electron redox potentials of the flavin to stabilize the semiquinone form.
About this Structure
1FRQ is a Single protein structure of sequence from Spinacia oleracea. Full crystallographic information is available from OCA.
Reference
Probing the function of the invariant glutamyl residue 312 in spinach ferredoxin-NADP+ reductase., Aliverti A, Deng Z, Ravasi D, Piubelli L, Karplus PA, Zanetti G, J Biol Chem. 1998 Dec 18;273(51):34008-15. PMID:9852055
Page seeded by OCA on Thu Mar 20 11:13:05 2008
