1gaw: Difference between revisions

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New page: left|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="450" color="white" frame="true" align="right" spinBox="true"
caption="1gaw, resolution 2.20&Aring;" />
'''CRYSTAL STRUCTURE ANALYSIS OF THE FERREDOXIN-NADP+ REDUCTASE FROM MAIZE LEAF'''<br />


==Overview==
==CRYSTAL STRUCTURE ANALYSIS OF THE FERREDOXIN-NADP+ REDUCTASE FROM MAIZE LEAF==
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.
<StructureSection load='1gaw' size='340' side='right'caption='[[1gaw]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1gaw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Zea_mays Zea mays]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GAW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GAW FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gaw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gaw OCA], [https://pdbe.org/1gaw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gaw RCSB], [https://www.ebi.ac.uk/pdbsum/1gaw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gaw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9SLP6_MAIZE Q9SLP6_MAIZE]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ga/1gaw_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1gaw ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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==
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<ref>PMID:11175898</ref>
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GAW OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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]
</div>
[[Category: Ferredoxin--NADP(+) reductase]]
<div class="pdbe-citations 1gaw" style="background-color:#fffaf0;"></div>
[[Category: Single protein]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Zea mays]]
[[Category: Zea mays]]
[[Category: Hase, T.]]
[[Category: Hase T]]
[[Category: Kurisu, G.]]
[[Category: Kurisu G]]
[[Category: Kusunoki, M.]]
[[Category: Kusunoki M]]
[[Category: FAD]]
[[Category: oxidoreductase/electron transport]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 01:07:33 2007''

Latest revision as of 02:29, 28 December 2023

CRYSTAL STRUCTURE ANALYSIS OF THE FERREDOXIN-NADP+ REDUCTASE FROM MAIZE LEAFCRYSTAL STRUCTURE ANALYSIS OF THE FERREDOXIN-NADP+ REDUCTASE FROM MAIZE LEAF

Structural highlights

1gaw is a 2 chain structure with sequence from Zea mays. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q9SLP6_MAIZE

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Kurisu G, Kusunoki M, Katoh E, Yamazaki T, Teshima K, Onda Y, Kimata-Ariga Y, Hase T. Structure of the electron transfer complex between ferredoxin and ferredoxin-NADP(+) reductase. Nat Struct Biol. 2001 Feb;8(2):117-21. PMID:11175898 doi:http://dx.doi.org/10.1038/84097

1gaw, resolution 2.20Å

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