1a70: Difference between revisions
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<StructureSection load='1a70' size='340' side='right'caption='[[1a70]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='1a70' size='340' side='right'caption='[[1a70]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1a70]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <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='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> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</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> | <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> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Spinacia oleracea]] | ||
[[Category: Aliverti | [[Category: Aliverti A]] | ||
[[Category: Binda | [[Category: Binda C]] | ||
[[Category: Coda | [[Category: Coda A]] | ||
[[Category: Mattevi | [[Category: Mattevi A]] | ||
[[Category: Zanetti | [[Category: Zanetti G]] | ||
Latest revision as of 13:48, 2 August 2023
SPINACH FERREDOXINSPINACH FERREDOXIN
Structural highlights
FunctionFER1_SPIOL Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. 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 PubMedFerredoxin 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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