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==NMR STUDY OF 2FE-2S FERREDOXIN OF SYNECHOCOCCUS ELONGATUS==
==NMR STUDY OF 2FE-2S FERREDOXIN OF SYNECHOCOCCUS ELONGATUS==
<StructureSection load='1roe' size='340' side='right'caption='[[1roe]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
<StructureSection load='1roe' size='340' side='right'caption='[[1roe]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1roe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechococcus_elongatus Synechococcus elongatus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ROE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ROE FirstGlance]. <br>
<table><tr><td colspan='2'>[[1roe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechococcus_elongatus Synechococcus elongatus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ROE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ROE 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">Solution NMR</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=1roe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1roe OCA], [https://pdbe.org/1roe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1roe RCSB], [https://www.ebi.ac.uk/pdbsum/1roe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1roe 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=1roe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1roe OCA], [https://pdbe.org/1roe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1roe RCSB], [https://www.ebi.ac.uk/pdbsum/1roe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1roe ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/FER_SYNEL FER_SYNEL]] Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.  
[https://www.uniprot.org/uniprot/FER_THEVB FER_THEVB] 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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</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=1roe ConSurf].
</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=1roe ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Ferredoxins of the [Fe2S2] type function in photosynthetic electron transport as essential electron acceptors of photosystem I. The solution structure of the 97 amino acid ferredoxin from the thermophilic cyanobacterium Synechococcus elongatus was determined by nuclear magnetic resonance spectroscopy and restrained molecular dynamics calculations. The structure consists of a four-stranded parallel/ antiparallel beta-sheet, a short two-stranded antiparallel beta-sheet, and three short helices. The overall structure is similar to the structure of the ferredoxin from Anabaena. In contrast to related ferredoxins from mesophilic organisms, this thermostable protein contains a salt bridge inside a 17-amino acid hydrophobic core.
Structure of Synechococcus elongatus [Fe2S2] ferredoxin in solution.,Baumann B, Sticht H, Scharpf M, Sutter M, Haehnel W, Rosch P Biochemistry. 1996 Oct 1;35(39):12831-41. PMID:8841126<ref>PMID:8841126</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1roe" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Ferredoxin 3D structures|Ferredoxin 3D structures]]
*[[Ferredoxin 3D structures|Ferredoxin 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Synechococcus elongatus]]
[[Category: Synechococcus elongatus]]
[[Category: Baumann, B]]
[[Category: Baumann B]]
[[Category: Haehnel, W]]
[[Category: Haehnel W]]
[[Category: Roesch, P]]
[[Category: Roesch P]]
[[Category: Sticht, H]]
[[Category: Sticht H]]
[[Category: Sutter, M]]
[[Category: Sutter M]]
[[Category: Electron transport]]
[[Category: Iron-sulfur]]

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