1qfz
From Proteopedia
(New page: 200px<br /><applet load="1qfz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qfz, resolution 1.7Å" /> '''PEA FNR Y308S MUTANT ...) |
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| - | [[Image:1qfz.gif|left|200px]]<br /><applet load="1qfz" size=" | + | [[Image:1qfz.gif|left|200px]]<br /><applet load="1qfz" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1qfz, resolution 1.7Å" /> | caption="1qfz, resolution 1.7Å" /> | ||
'''PEA FNR Y308S MUTANT IN COMPLEX WITH NADPH'''<br /> | '''PEA FNR Y308S MUTANT IN COMPLEX WITH NADPH'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The flavoenzyme ferredoxin-NADP+ reductase (FNR) catalyzes the production | + | 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== | ==About this Structure== | ||
| - | 1QFZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum] with SO4, FAD and NDP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | + | 1QFZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=FAD:'>FAD</scene> and <scene name='pdbligand=NDP:'>NDP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QFZ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Aliverti, A.]] | [[Category: Aliverti, A.]] | ||
| - | [[Category: Arakaki, A | + | [[Category: Arakaki, A K.]] |
| - | [[Category: Calcaterra, N | + | [[Category: Calcaterra, N B.]] |
[[Category: Carrillo, N.]] | [[Category: Carrillo, N.]] | ||
| - | [[Category: Ceccarelli, E | + | [[Category: Ceccarelli, E A.]] |
[[Category: Deng, Z.]] | [[Category: Deng, Z.]] | ||
| - | [[Category: Karplus, P | + | [[Category: Karplus, P A.]] |
| - | [[Category: Orellano, E | + | [[Category: Orellano, E G.]] |
[[Category: Ottado, J.]] | [[Category: Ottado, J.]] | ||
[[Category: Zanetti, G.]] | [[Category: Zanetti, G.]] | ||
| Line 32: | Line 32: | ||
[[Category: photosynthesis]] | [[Category: photosynthesis]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:39:04 2008'' |
Revision as of 12:39, 21 February 2008
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PEA FNR Y308S MUTANT IN COMPLEX WITH NADPH
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
1QFZ is a Single protein structure of sequence from Pisum sativum with , and as ligands. Active as Ferredoxin--NADP(+) reductase, with EC number 1.18.1.2 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 Thu Feb 21 14:39:04 2008
Categories: Ferredoxin--NADP(+) reductase | Pisum sativum | Single protein | Aliverti, A. | Arakaki, A K. | Calcaterra, N B. | Carrillo, N. | Ceccarelli, E A. | Deng, Z. | Karplus, P A. | Orellano, E G. | Ottado, J. | Zanetti, G. | FAD | NDP | SO4 | Electron transfer | Flavoenzyme | Hydride transfer | Photosynthesis
