1w34

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[[Image:1w34.gif|left|200px]]
[[Image:1w34.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1w34 |SIZE=350|CAPTION= <scene name='initialview01'>1w34</scene>, resolution 1.73&Aring;
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The line below this paragraph, containing "STRUCTURE_1w34", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+A'>AC1</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|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>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1w34| PDB=1w34 | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1w34 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w34 OCA], [http://www.ebi.ac.uk/pdbsum/1w34 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1w34 RCSB]</span>
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}}
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'''FERREDOXIN-NADP REDUCTASE (MUTATION: Y 303 S)'''
'''FERREDOXIN-NADP REDUCTASE (MUTATION: Y 303 S)'''
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C-terminal tyrosine of ferredoxin-NADP+ reductase in hydride transfer processes with NAD(P)+/H., Tejero J, Perez-Dorado I, Maya C, Martinez-Julvez M, Sanz-Aparicio J, Gomez-Moreno C, Hermoso JA, Medina M, Biochemistry. 2005 Oct 18;44(41):13477-90. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16216071 16216071]
C-terminal tyrosine of ferredoxin-NADP+ reductase in hydride transfer processes with NAD(P)+/H., Tejero J, Perez-Dorado I, Maya C, Martinez-Julvez M, Sanz-Aparicio J, Gomez-Moreno C, Hermoso JA, Medina M, Biochemistry. 2005 Oct 18;44(41):13477-90. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16216071 16216071]
[[Category: Anabaena sp.]]
[[Category: Anabaena sp.]]
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[[Category: Ferredoxin--NADP(+) reductase]]
 
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Gomez-Moreno, C.]]
[[Category: Gomez-Moreno, C.]]
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[[Category: Sanz-Aparicio, J.]]
[[Category: Sanz-Aparicio, J.]]
[[Category: 3d-structure]]
[[Category: 3d-structure]]
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[[Category: fad]]
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[[Category: Fad]]
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[[Category: flavoprotein]]
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[[Category: Flavoprotein]]
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[[Category: fnr]]
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[[Category: Fnr]]
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[[Category: membrane]]
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[[Category: Membrane]]
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[[Category: nadp]]
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[[Category: Nadp]]
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[[Category: nadp reductase]]
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[[Category: Nadp reductase]]
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[[Category: oxidoreductase]]
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[[Category: Oxidoreductase]]
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[[Category: phycobilisome]]
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[[Category: Phycobilisome]]
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[[Category: thylakoid]]
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[[Category: Thylakoid]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:05:27 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:30:31 2008''
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Revision as of 10:05, 3 May 2008

Image:1w34.gif

Template:STRUCTURE 1w34

FERREDOXIN-NADP REDUCTASE (MUTATION: Y 303 S)


Overview

Ferredoxin-NADP+ reductase (FNR) catalyzes the reduction of NADP+ to NADPH in an overall reversible reaction, showing some differences in the mechanisms between cyanobacterial and higher plant FNRs. During hydride transfer it is proposed that the FNR C-terminal Tyr is displaced by the nicotinamide. Thus, this C-terminal Tyr might be involved not only in modulating the flavin redox properties, as already shown, but also in nicotinamide binding and hydride transfer. FNR variants from the cyanobacterium Anabaena in which the C-terminal Tyr has been replaced by Trp, Phe, or Ser have been produced. All FNR variants show enhanced NADP+ and NAD+ binding, especially Tyr303Ser, which correlates with a noticeable improvement of NADH-dependent reactions. Nevertheless, the Tyr303Ser variant shows a decrease in the steady-state kcat value with NADPH. Fast kinetic analysis of the hydride transfer shows that the low efficiency observed for this mutant FNR under steady-state conditions is not due to a lack of catalytic ability but rather to the strong enzyme-coenzyme interaction. Three-dimensional structures for Tyr303Ser and Tyr303Trp variants and its complexes with NADP+ show significant differences between plant and cyanobacterial FNRs. Our results suggest that modulation of coenzyme affinity is highly influenced by the strength of the C-terminus-FAD interaction and that subtle changes between plant and cyanobacterial structures are able to modify the energy of that interaction. Additionally, it is shown that the C-terminal Tyr of FNR lowers the affinity for NADP+/H to levels compatible with steady-state turnover during the catalytic cycle, but it is not involved in the hydride transfer itself.

About this Structure

1W34 is a Single protein structure of sequence from Anabaena sp.. Full crystallographic information is available from OCA.

Reference

C-terminal tyrosine of ferredoxin-NADP+ reductase in hydride transfer processes with NAD(P)+/H., Tejero J, Perez-Dorado I, Maya C, Martinez-Julvez M, Sanz-Aparicio J, Gomez-Moreno C, Hermoso JA, Medina M, Biochemistry. 2005 Oct 18;44(41):13477-90. PMID:16216071 Page seeded by OCA on Sat May 3 13:05:27 2008

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