1gaw
From Proteopedia
(New page: 200px<br /><applet load="1gaw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gaw, resolution 2.20Å" /> '''CRYSTAL STRUCTURE AN...) |
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| - | [[Image:1gaw.gif|left|200px]]<br /><applet load="1gaw" size=" | + | [[Image:1gaw.gif|left|200px]]<br /><applet load="1gaw" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1gaw, resolution 2.20Å" /> | caption="1gaw, resolution 2.20Å" /> | ||
'''CRYSTAL STRUCTURE ANALYSIS OF THE FERREDOXIN-NADP+ REDUCTASE FROM MAIZE LEAF'''<br /> | '''CRYSTAL STRUCTURE ANALYSIS OF THE FERREDOXIN-NADP+ REDUCTASE FROM MAIZE LEAF'''<br /> | ||
==Overview== | ==Overview== | ||
| - | All oxygenic photosynthetically derived reducing equivalents are utilized | + | 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== | ==About this Structure== | ||
| - | 1GAW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Zea_mays Zea mays] 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:// | + | 1GAW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Zea_mays Zea mays] 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=1GAW OCA]. |
==Reference== | ==Reference== | ||
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[[Category: oxidoreductase/electron transport]] | [[Category: oxidoreductase/electron transport]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:48:04 2008'' |
Revision as of 10:48, 21 February 2008
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CRYSTAL STRUCTURE ANALYSIS OF THE FERREDOXIN-NADP+ REDUCTASE FROM MAIZE LEAF
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
1GAW is a Single protein structure of sequence from Zea mays with as ligand. Active as Ferredoxin--NADP(+) reductase, with EC number 1.18.1.2 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
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