1gaq

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1gaq.gif|left|200px]]<br /><applet load="1gaq" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1gaq.gif|left|200px]]
-
caption="1gaq, resolution 2.59&Aring;" />
+
 
-
'''CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN FERREDOXIN AND FERREDOXIN-NADP+ REDUCTASE'''<br />
+
{{Structure
 +
|PDB= 1gaq |SIZE=350|CAPTION= <scene name='initialview01'>1gaq</scene>, resolution 2.59&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene> and <scene name='pdbligand=FES:FE2/S2 (INORGANIC) CLUSTER'>FES</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=
 +
}}
 +
 
 +
'''CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN FERREDOXIN AND FERREDOXIN-NADP+ REDUCTASE'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
1GAQ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Zea_mays Zea mays] with <scene name='pdbligand=FAD:'>FAD</scene> and <scene name='pdbligand=FES:'>FES</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=1GAQ OCA].
+
1GAQ is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Zea_mays Zea mays]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GAQ OCA].
==Reference==
==Reference==
-
Structure of the electron transfer complex between ferredoxin and ferredoxin-NADP(+) reductase., Kurisu G, Kusunoki M, Katoh E, Yamazaki T, Teshima K, Onda Y, Kimata-Ariga Y, Hase T, Nat Struct Biol. 2001 Feb;8(2):117-21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11175898 11175898]
+
Structure of the electron transfer complex between ferredoxin and ferredoxin-NADP(+) reductase., Kurisu G, Kusunoki M, Katoh E, Yamazaki T, Teshima K, Onda Y, Kimata-Ariga Y, Hase T, Nat Struct Biol. 2001 Feb;8(2):117-21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11175898 11175898]
[[Category: Ferredoxin--NADP(+) reductase]]
[[Category: Ferredoxin--NADP(+) reductase]]
[[Category: Protein complex]]
[[Category: Protein complex]]
Line 21: Line 30:
[[Category: oxidoreductase/electron transport]]
[[Category: oxidoreductase/electron transport]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:48:04 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:20:39 2008''

Revision as of 09:20, 20 March 2008


PDB ID 1gaq

Drag the structure with the mouse to rotate
, resolution 2.59Å
Ligands: and
Activity: Ferredoxin--NADP(+) reductase, with EC number 1.18.1.2
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN FERREDOXIN AND FERREDOXIN-NADP+ REDUCTASE


Overview

All oxygenic photosynthetically derived reducing equivalents are utilized by combinations of a single multifuctional electron carrier protein, ferredoxin (Fd), and several Fd-dependent oxidoreductases. We report the first crystal structure of the complex between maize leaf Fd and Fd-NADP(+) oxidoreductase (FNR). The redox centers in the complex--the 2Fe-2S cluster of Fd and flavin adenine dinucleotide (FAD) of FNR--are in close proximity; the shortest distance is 6.0 A. The intermolecular interactions in the complex are mainly electrostatic, occurring through salt bridges, and the interface near the prosthetic groups is hydrophobic. NMR experiments on the complex in solution confirmed the FNR recognition sites on Fd that are identified in the crystal structure. Interestingly, the structures of Fd and FNR in the complex and in the free state differ in several ways. For example, in the active site of FNR, Fd binding induces the formation of a new hydrogen bond between side chains of Glu 312 and Ser 96 of FNR. We propose that this type of molecular communication not only determines the optimal orientation of the two proteins for electron transfer, but also contributes to the modulation of the enzymatic properties of FNR.

About this Structure

1GAQ is a Protein complex structure of sequences from Zea mays. Full crystallographic information is available from OCA.

Reference

Structure of the electron transfer complex between ferredoxin and ferredoxin-NADP(+) reductase., Kurisu G, Kusunoki M, Katoh E, Yamazaki T, Teshima K, Onda Y, Kimata-Ariga Y, Hase T, Nat Struct Biol. 2001 Feb;8(2):117-21. PMID:11175898

Page seeded by OCA on Thu Mar 20 11:20:39 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools