2cjn
From Proteopedia
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| - | [[Image:2cjn.gif|left|200px]]<br /><applet load="2cjn" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2cjn" /> | ||
| - | '''STRUCTURE OF FERREDOXIN, NMR, MINIMIZED AVERAGE STRUCTURE'''<br /> | ||
| - | == | + | ==STRUCTURE OF FERREDOXIN, NMR, MINIMIZED AVERAGE STRUCTURE== |
| + | <StructureSection load='2cjn' size='340' side='right'caption='[[2cjn]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2cjn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechococcus_elongatus Synechococcus elongatus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1cjn 1cjn]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CJN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CJN FirstGlance]. <br> | ||
| + | </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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2cjn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cjn OCA], [https://pdbe.org/2cjn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cjn RCSB], [https://www.ebi.ac.uk/pdbsum/2cjn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cjn ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [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 == | ||
| + | [[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/cj/2cjn_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=2cjn ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
The three-dimensional structure of ferredoxin, purified from the thermophilic cyanobacterium Synechococcus elongatus, was determined in aqueous solution by two-dimensional proton nuclear magnetic resonance. In addition to the 946 distance constraints from nuclear Overhauser effect connectivities, we added 241 distance constraints derived from the crystal structure of Spirulina platensis ferredoxin to the 19 residues close to the [2Fe-2S] iron-sulfur center, where crosspeaks disappeared due to paramagnetic effects. The atomic root-mean-square difference of the ten converged structures from the mean structure was 0.61(+/-0.12) A for backbone atoms (N, C(alpha), C'). The main-chain structure was almost the same as the crystal structures of other mesophile ferredoxins, but comparison of the side-chain structures revealed an extension of the hydrophobic core, a unique hydrophobic patch on the surface of the large beta-sheet, and two unique charge networks in this thermostable ferredoxin structure, some of which might contribute to thermostability. | The three-dimensional structure of ferredoxin, purified from the thermophilic cyanobacterium Synechococcus elongatus, was determined in aqueous solution by two-dimensional proton nuclear magnetic resonance. In addition to the 946 distance constraints from nuclear Overhauser effect connectivities, we added 241 distance constraints derived from the crystal structure of Spirulina platensis ferredoxin to the 19 residues close to the [2Fe-2S] iron-sulfur center, where crosspeaks disappeared due to paramagnetic effects. The atomic root-mean-square difference of the ten converged structures from the mean structure was 0.61(+/-0.12) A for backbone atoms (N, C(alpha), C'). The main-chain structure was almost the same as the crystal structures of other mesophile ferredoxins, but comparison of the side-chain structures revealed an extension of the hydrophobic core, a unique hydrophobic patch on the surface of the large beta-sheet, and two unique charge networks in this thermostable ferredoxin structure, some of which might contribute to thermostability. | ||
| - | + | Solution structure of ferredoxin from the thermophilic cyanobacterium Synechococcus elongatus and its thermostability.,Hatanaka H, Tanimura R, Katoh S, Inagaki F J Mol Biol. 1997 May 23;268(5):922-33. PMID:9180381<ref>PMID:9180381</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2cjn" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Ferredoxin 3D structures|Ferredoxin 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Synechococcus elongatus]] | ||
| + | [[Category: Hatanaka H]] | ||
| + | [[Category: Inagaki F]] | ||
| + | [[Category: Katoh S]] | ||
| + | [[Category: Tanimura R]] | ||
Current revision
STRUCTURE OF FERREDOXIN, NMR, MINIMIZED AVERAGE STRUCTURE
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