1qg0

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(New page: 200px<br /><applet load="1qg0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qg0, resolution 2.5&Aring;" /> '''WILD-TYPE PEA FNR'''<...)
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[[Image:1qg0.gif|left|200px]]<br /><applet load="1qg0" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1qg0, resolution 2.5&Aring;" />
caption="1qg0, resolution 2.5&Aring;" />
'''WILD-TYPE PEA FNR'''<br />
'''WILD-TYPE PEA FNR'''<br />
==Overview==
==Overview==
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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.
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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==
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1QG0 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 FAD as [http://en.wikipedia.org/wiki/ligand ligand]. 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QG0 OCA].
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1QG0 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=FAD:'>FAD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1QG0 OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Aliverti, A.]]
[[Category: Aliverti, A.]]
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[[Category: Arakaki, A.K.]]
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[[Category: Arakaki, A K.]]
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[[Category: Calcaterra, N.B.]]
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[[Category: Calcaterra, N B.]]
[[Category: Carrillo, N.]]
[[Category: Carrillo, N.]]
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[[Category: Ceccarelli, E.A.]]
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[[Category: Ceccarelli, E A.]]
[[Category: Deng, Z.]]
[[Category: Deng, Z.]]
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[[Category: Karplus, P.A.]]
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[[Category: Karplus, P A.]]
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[[Category: Orellano, E.G.]]
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[[Category: Orellano, E G.]]
[[Category: Ottado, J.]]
[[Category: Ottado, J.]]
[[Category: Zanetti, G.]]
[[Category: Zanetti, G.]]
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[[Category: photosynthesis]]
[[Category: photosynthesis]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:39:25 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:39:05 2008''

Revision as of 12:39, 21 February 2008


1qg0, resolution 2.5Å

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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 with as ligand. 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

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