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[[Image:1a70.gif|left|200px]]
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{{STRUCTURE_1a70|  PDB=1a70  |  SCENE=  }}
'''SPINACH FERREDOXIN'''


==SPINACH FERREDOXIN==
<StructureSection load='1a70' size='340' side='right'caption='[[1a70]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1a70]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A70 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A70 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]] 1.7&#8491;</td></tr>
<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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1a70 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a70 OCA], [https://pdbe.org/1a70 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a70 RCSB], [https://www.ebi.ac.uk/pdbsum/1a70 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a70 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FER1_SPIOL FER1_SPIOL] Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
== 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/a7/1a70_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=1a70 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Ferredoxin I (Fd I) from Spinacia oleracea is composed of 97 amino-acid residues and a [2Fe-2S] cluster. The crystal structure of the E92K mutant of Fd I was solved by molecular replacement and refined to an R factor of 19.6% for 11755 reflections at 1.7 A resolution. The overall structure and the active centre of spinach Fd is highly conserved with respect to ferredoxins of known structure. The E92K mutation appears to disturb a hydrogen-bond network which stabilizes the loop bearing the [2Fe-2S] cluster. This observation provides a rationale for the reduced electron-transfer efficiency displayed by the E92K mutant. Inspection of the crystal packing reveals that the side chain of Lys92 is engaged in an intermolecular interaction with Asp26 of a symmetry-related molecule. This feature may explain why only the mutant E92K and not wild-type Fd I could be successfully crystallized.


==Overview==
Structure of the mutant E92K of [2Fe-2S] ferredoxin I from Spinacia oleracea at 1.7 A resolution.,Binda C, Coda A, Aliverti A, Zanetti G, Mattevi A Acta Crystallogr D Biol Crystallogr. 1998 Nov 1;54(Pt 6 Pt 2):1353-8. PMID:10089511<ref>PMID:10089511</ref>
Ferredoxin I (Fd I) from Spinacia oleracea is composed of 97 amino-acid residues and a [2Fe-2S] cluster. The crystal structure of the E92K mutant of Fd I was solved by molecular replacement and refined to an R factor of 19.6% for 11755 reflections at 1.7 A resolution. The overall structure and the active centre of spinach Fd is highly conserved with respect to ferredoxins of known structure. The E92K mutation appears to disturb a hydrogen-bond network which stabilizes the loop bearing the [2Fe-2S] cluster. This observation provides a rationale for the reduced electron-transfer efficiency displayed by the E92K mutant. Inspection of the crystal packing reveals that the side chain of Lys92 is engaged in an intermolecular interaction with Asp26 of a symmetry-related molecule. This feature may explain why only the mutant E92K and not wild-type Fd I could be successfully crystallized.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1A70 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A70 OCA].
</div>
<div class="pdbe-citations 1a70" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Structure of the mutant E92K of [2Fe-2S] ferredoxin I from Spinacia oleracea at 1.7 A resolution., Binda C, Coda A, Aliverti A, Zanetti G, Mattevi A, Acta Crystallogr D Biol Crystallogr. 1998 Nov 1;54(Pt 6 Pt 2):1353-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10089511 10089511]
*[[Ferredoxin 3D structures|Ferredoxin 3D structures]]
[[Category: Single protein]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Spinacia oleracea]]
[[Category: Spinacia oleracea]]
[[Category: Aliverti, A.]]
[[Category: Aliverti A]]
[[Category: Binda, C.]]
[[Category: Binda C]]
[[Category: Coda, A.]]
[[Category: Coda A]]
[[Category: Mattevi, A.]]
[[Category: Mattevi A]]
[[Category: Zanetti, G.]]
[[Category: Zanetti G]]
[[Category: Electron transport]]
[[Category: Iron-sulfur protein]]
[[Category: Photosynthesis]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 09:54:32 2008''

Latest revision as of 05:19, 13 August 2026

SPINACH FERREDOXIN

1a70, resolution 1.70Å

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