3e6z

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{{Seed}}
 
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[[Image:3e6z.png|left|200px]]
 
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==1.0 A Structure of CusF-W44A-Cu(II) residues 10-88 from Escherichia coli==
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The line below this paragraph, containing "STRUCTURE_3e6z", creates the "Structure Box" on the page.
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<StructureSection load='3e6z' size='340' side='right'caption='[[3e6z]], [[Resolution|resolution]] 1.00&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3e6z]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E6Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E6Z FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</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&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr>
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{{STRUCTURE_3e6z| PDB=3e6z | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3e6z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e6z OCA], [https://pdbe.org/3e6z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e6z RCSB], [https://www.ebi.ac.uk/pdbsum/3e6z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e6z ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CUSF_ECOLI CUSF_ECOLI] Part of a cation efflux system that mediates resistance to copper and silver. Binds one copper per polypeptide.<ref>PMID:11399769</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e6/3e6z_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=3e6z ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The periplasmic metallochaperone CusF coordinates Cu(I) and Ag(I) through a unique site consisting of a Met(2)His motif as well as a Cu(I)-pi interaction between a nearby tryptophan, W44, and the metal ion. Through mutational analyses we investigate here the role that W44 in CusF plays in metal coordination. Nuclear magnetic resonance spectra show that the specificity of CusF for Cu(I) and Ag(I) is not altered by mutation of W44. X-ray absorption spectroscopy studies reveal that W44 protects the bound Cu(I) from oxidation as well as from adventitious ligands. Competition assays demonstrate that W44 does not significantly contribute to the affinity of CusF for metal, but that substitution of W44 by methionine, which forms a fourth Cu(I) ligand, substantially increases the affinity. These studies indicate that W44 is important in maintaining a moderate-affinity and solvent-shielded three-coordinate environment for Cu(I), which has implications for the function of CusF as a metallochaperone.
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===1.0 A Structure of CusF-W44A-Cu(II) residues 10-88 from Escherichia coli===
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Tryptophan Cu(I)-pi interaction fine-tunes the metal binding properties of the bacterial metallochaperone CusF.,Loftin IR, Blackburn NJ, McEvoy MM J Biol Inorg Chem. 2009 Apr 21. PMID:19381697<ref>PMID:19381697</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_19381697}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 3e6z" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 19381697 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_19381697}}
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__TOC__
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</StructureSection>
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==About this Structure==
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3E6Z is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E6Z OCA].
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==Reference==
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<ref group="xtra">PMID:19381697</ref><references group="xtra"/>
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Loftin, I R.]]
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[[Category: Large Structures]]
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[[Category: Beta-barrel]]
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[[Category: Loftin IR]]
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[[Category: Copper chaperone]]
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[[Category: Copper-binding]]
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[[Category: Metal binding protein]]
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[[Category: Metal resistance]]
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[[Category: Metal-binding]]
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[[Category: Metalloprotein]]
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[[Category: Ob-fold]]
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[[Category: Periplasm]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Aug 12 13:54:23 2009''
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Current revision

1.0 A Structure of CusF-W44A-Cu(II) residues 10-88 from Escherichia coli

PDB ID 3e6z

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