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[[Image:1i7h.gif|left|200px]]


{{Structure
==CRYSTAL STURCUTURE OF FDX==
|PDB= 1i7h |SIZE=350|CAPTION= <scene name='initialview01'>1i7h</scene>, resolution 1.70&Aring;
<StructureSection load='1i7h' size='340' side='right'caption='[[1i7h]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>
<table><tr><td colspan='2'>[[1i7h]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I7H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I7H FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1i7h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i7h OCA], [https://pdbe.org/1i7h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i7h RCSB], [https://www.ebi.ac.uk/pdbsum/1i7h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i7h ProSAT]</span></td></tr>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1i7h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i7h OCA], [http://www.ebi.ac.uk/pdbsum/1i7h PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1i7h RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/FER_ECOLI FER_ECOLI] Ferredoxin are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. Although the function of this ferredoxin is unknown it is probable that it has a role as a cellular electron transfer protein. Involved in the in vivo assembly of the Fe-S clusters in a wide variety of iron-sulfur proteins.
== 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/i7/1i7h_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1i7h ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Escherichia coli ferredoxin (Fdx) is an adrenodoxin-type [2Fe-2S] ferredoxin. Recent genetic analyses show that it has an essential role in the maturation of various iron-sulfur (Fe-S) proteins. Fdx probably functions as a component of the complex machinery responsible for the biogenesis of Fe-S clusters. Its crystal structure was determined by the multiple-wavelength anomalous dispersion method using the iron atoms in the [2Fe-2S] cluster of the protein and then refined to R and R(free) values of 0.255 and 0.278, respectively, at 1.7 A resolution. The structure of Fdx is similar to the structures of bovine adrenodoxin (Adx) and Pseudomonas putida putidaredoxin (Pdx) whose respective root-mean-square deviations of the corresponding Calpha atoms are 1.8 and 2.2 A. This analysis also revealed the structure of the C-terminal residues protruding into the solvent, which is missing in Adx and Pdx. The [2Fe-2S] cluster is located at the edge of the molecule and bonds with the Sgamma atoms of Cys42, Cys48, Cys51, and Cys87. Electrostatic potential analysis showed that the surface of Fdx has two negatively charged areas separated by a hydrophobic lane. One is conserved on the surface of Adx which is an area of interaction with adrenodoxin reductase. Cys46 is located on the molecular surface in the vicinity of the [2Fe-2S] cluster, an indication that it may be involved in Fe-S cluster formation.


'''CRYSTAL STURCUTURE OF FDX'''
Crystal structure of Escherichia coli Fdx, an adrenodoxin-type ferredoxin involved in the assembly of iron-sulfur clusters.,Kakuta Y, Horio T, Takahashi Y, Fukuyama K Biochemistry. 2001 Sep 18;40(37):11007-12. PMID:11551196<ref>PMID:11551196</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1i7h" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
Escherichia coli ferredoxin (Fdx) is an adrenodoxin-type [2Fe-2S] ferredoxin. Recent genetic analyses show that it has an essential role in the maturation of various iron-sulfur (Fe-S) proteins. Fdx probably functions as a component of the complex machinery responsible for the biogenesis of Fe-S clusters. Its crystal structure was determined by the multiple-wavelength anomalous dispersion method using the iron atoms in the [2Fe-2S] cluster of the protein and then refined to R and R(free) values of 0.255 and 0.278, respectively, at 1.7 A resolution. The structure of Fdx is similar to the structures of bovine adrenodoxin (Adx) and Pseudomonas putida putidaredoxin (Pdx) whose respective root-mean-square deviations of the corresponding Calpha atoms are 1.8 and 2.2 A. This analysis also revealed the structure of the C-terminal residues protruding into the solvent, which is missing in Adx and Pdx. The [2Fe-2S] cluster is located at the edge of the molecule and bonds with the Sgamma atoms of Cys42, Cys48, Cys51, and Cys87. Electrostatic potential analysis showed that the surface of Fdx has two negatively charged areas separated by a hydrophobic lane. One is conserved on the surface of Adx which is an area of interaction with adrenodoxin reductase. Cys46 is located on the molecular surface in the vicinity of the [2Fe-2S] cluster, an indication that it may be involved in Fe-S cluster formation.
*[[Ferredoxin|Ferredoxin]]
 
*[[Ferredoxin 3D structures|Ferredoxin 3D structures]]
==About this Structure==
*[[Iron–sulfur proteins|Iron–sulfur proteins]]
1I7H is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I7H OCA].
== References ==
 
<references/>
==Reference==
__TOC__
Crystal structure of Escherichia coli Fdx, an adrenodoxin-type ferredoxin involved in the assembly of iron-sulfur clusters., Kakuta Y, Horio T, Takahashi Y, Fukuyama K, Biochemistry. 2001 Sep 18;40(37):11007-12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11551196 11551196]
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Fukuyama, K.]]
[[Category: Fukuyama K]]
[[Category: Horio, T.]]
[[Category: Horio T]]
[[Category: Kakuta, Y.]]
[[Category: Kakuta Y]]
[[Category: Takahashi, Y.]]
[[Category: Takahashi Y]]
[[Category: 2fe-2s,electron transport]]
 
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Retrieved from "https://proteopedia.org/1i7h"