2vb3

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(New page: 200px<br /><applet load="2vb3" size="350" color="white" frame="true" align="right" spinBox="true" caption="2vb3, resolution 2.33&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:2vb3.jpg|left|200px]]<br /><applet load="2vb3" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2vb3, resolution 2.33&Aring;" />
 
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'''CRYSTAL STRUCTURE OF AG(I)CUSF'''<br />
 
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==Overview==
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==Crystal structure of Ag(I)CusF==
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Methionine-rich motifs have an important role in copper trafficking, factors, including the CusF protein. Here we show that CusF uses a new, metal recognition site wherein Cu(I) is tetragonally displaced from a, Met2His ligand plane toward a conserved tryptophan. Spectroscopic studies, demonstrate that both thioether ligation and strong cation-pi interactions, with tryptophan stabilize metal binding. This novel active site chemistry, affords mechanisms for control of adventitious metal redox and, substitution chemistry.
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<StructureSection load='2vb3' size='340' side='right'caption='[[2vb3]], [[Resolution|resolution]] 2.33&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2vb3]] 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=2VB3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VB3 FirstGlance]. <br>
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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]] 2.33&#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=AG:SILVER+ION'>AG</scene></td></tr>
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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=2vb3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vb3 OCA], [https://pdbe.org/2vb3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vb3 RCSB], [https://www.ebi.ac.uk/pdbsum/2vb3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vb3 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/vb/2vb3_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=2vb3 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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Methionine-rich motifs have an important role in copper trafficking factors, including the CusF protein. Here we show that CusF uses a new metal recognition site wherein Cu(I) is tetragonally displaced from a Met2His ligand plane toward a conserved tryptophan. Spectroscopic studies demonstrate that both thioether ligation and strong cation-pi interactions with tryptophan stabilize metal binding. This novel active site chemistry affords mechanisms for control of adventitious metal redox and substitution chemistry.
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==About this Structure==
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Cu(I) recognition via cation-pi and methionine interactions in CusF.,Xue Y, Davis AV, Balakrishnan G, Stasser JP, Staehlin BM, Focia P, Spiro TG, Penner-Hahn JE, O'Halloran TV Nat Chem Biol. 2008 Feb;4(2):107-9. Epub 2007 Dec 23. PMID:18157124<ref>PMID:18157124</ref>
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2VB3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=AG:'>AG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Ag Binding Site For Chain X'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VB3 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Cu(I) recognition via cation-pi and methionine interactions in CusF., Xue Y, Davis AV, Balakrishnan G, Stasser JP, Staehlin BM, Focia P, Spiro TG, Penner-Hahn JE, O'Halloran TV, Nat Chem Biol. 2008 Feb;4(2):107-9. Epub 2007 Dec 23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18157124 18157124]
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</div>
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<div class="pdbe-citations 2vb3" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Balakrishnan, G.]]
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[[Category: Balakrishnan G]]
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[[Category: Davis, A.V.]]
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[[Category: Davis AV]]
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[[Category: Focia, P.]]
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[[Category: Focia P]]
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[[Category: Halloran, T.V.O.]]
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[[Category: O'Halloran TV]]
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[[Category: Penner-Hahn, J.E.]]
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[[Category: Penner-Hahn JE]]
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[[Category: Spiro, T.G.]]
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[[Category: Spiro TG]]
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[[Category: Staehlin, B.M.]]
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[[Category: Staehlin BM]]
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[[Category: Stasser, J.P.]]
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[[Category: Stasser JP]]
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[[Category: Xue, Y.]]
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[[Category: Xue Y]]
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[[Category: AG]]
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[[Category: cation pi]]
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[[Category: copper]]
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[[Category: copper tolerance]]
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[[Category: copper transport]]
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[[Category: metal transport]]
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[[Category: metal-binding]]
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[[Category: periplasm]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:13:52 2008''
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Current revision

Crystal structure of Ag(I)CusF

PDB ID 2vb3

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