1w87

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1w87.gif|left|200px]]<br /><applet load="1w87" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1w87.gif|left|200px]]
-
caption="1w87, resolution 3.00&Aring;" />
+
 
-
'''FERREDOXIN-NADP REDUCTASE (MUTATION: Y 303 W) COMPLEXED WITH NADP BY COCRYSTALLIZATION'''<br />
+
{{Structure
 +
|PDB= 1w87 |SIZE=350|CAPTION= <scene name='initialview01'>1w87</scene>, resolution 3.00&Aring;
 +
|SITE= <scene name='pdbsite=AC1:Nap+Binding+Site+For+Chain+B'>AC1</scene>
 +
|LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene> and <scene name='pdbligand=NAP:NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE'>NAP</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 REDUCTASE (MUTATION: Y 303 W) COMPLEXED WITH NADP BY COCRYSTALLIZATION'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
1W87 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Anabaena_sp. Anabaena sp.] with <scene name='pdbligand=FAD:'>FAD</scene> and <scene name='pdbligand=NAP:'>NAP</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] Known structural/functional Site: <scene name='pdbsite=AC1:Nap+Binding+Site+For+Chain+B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W87 OCA].
+
1W87 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Anabaena_sp. Anabaena sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W87 OCA].
==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=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.]]
[[Category: Ferredoxin--NADP(+) reductase]]
[[Category: Ferredoxin--NADP(+) reductase]]
Line 29: Line 38:
[[Category: thylakoid]]
[[Category: thylakoid]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:41:28 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:53:28 2008''

Revision as of 12:53, 20 March 2008

Image:1w87.gif


PDB ID 1w87

Drag the structure with the mouse to rotate
, resolution 3.00Å
Sites:
Ligands: and
Activity: Ferredoxin--NADP(+) reductase, with EC number 1.18.1.2
Coordinates: save as pdb, mmCIF, xml



FERREDOXIN-NADP REDUCTASE (MUTATION: Y 303 W) COMPLEXED WITH NADP BY COCRYSTALLIZATION


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

1W87 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 Thu Mar 20 14:53:28 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1w87"
Personal tools