2p1x: Difference between revisions
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==Crystal structure analysis of the complex between CyaY and Eu(III)== | ==Crystal structure analysis of the complex between CyaY and Eu(III)== | ||
<StructureSection load='2p1x' size='340' side='right' caption='[[2p1x]], [[Resolution|resolution]] 1.42Å' scene=''> | <StructureSection load='2p1x' size='340' side='right' caption='[[2p1x]], [[Resolution|resolution]] 1.42Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2eff|2eff]], [[1soy|1soy]], [[1ew4|1ew4]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2eff|2eff]], [[1soy|1soy]], [[1ew4|1ew4]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cyaY ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cyaY ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2p1x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p1x OCA], [http://pdbe.org/2p1x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2p1x RCSB], [http://www.ebi.ac.uk/pdbsum/2p1x PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2p1x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p1x OCA], [http://pdbe.org/2p1x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2p1x RCSB], [http://www.ebi.ac.uk/pdbsum/2p1x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2p1x ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p1/2p1x_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p1/2p1x_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
Revision as of 10:15, 22 August 2018
Crystal structure analysis of the complex between CyaY and Eu(III)Crystal structure analysis of the complex between CyaY and Eu(III)
Structural highlights
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 PubMedDeficiency of the small mitochondrial protein frataxin causes Friedreich's ataxia, a severe neurodegenerative pathology. Frataxin, which has been highly conserved throughout evolution, is thought to be involved in, among other processes, Fe-S cluster formation. Independent evidence shows that it binds iron directly, although with very distinct features and low affinity. Here, we have carried out an extensive study of the binding properties of CyaY, the bacterial ortholog of frataxin, to different divalent and trivalent cations, using NMR and X-ray crystallography. We demonstrate that the protein has low cation specificity and contains multiple binding sites able to chelate divalent and trivalent metals with low affinity. Binding does not involve cavities or pockets, but exposed glutamates and aspartates, which are residues that are unusual for iron chelation when not assisted by histidines and/or cysteines. We have related how such an ability to bind cations on a relatively large area through an electrostatic mechanism could be a valuable asset for protein function. Understanding the binding properties of an unusual metal-binding protein--a study of bacterial frataxin.,Pastore C, Franzese M, Sica F, Temussi P, Pastore A FEBS J. 2007 Aug;274(16):4199-210. Epub 2007 Jul 25. PMID:17651435[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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