1lyq

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(New page: 200px<br /><applet load="1lyq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lyq, resolution 1.5&Aring;" /> '''Crystal Structure of ...)
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[[Image:1lyq.jpg|left|200px]]<br /><applet load="1lyq" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1lyq, resolution 1.5&Aring;" />
 
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'''Crystal Structure of PcoC, a Methionine Rich Copper Resistance Protein from Escherichia coli'''<br />
 
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==Overview==
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==Crystal Structure of PcoC, a Methionine Rich Copper Resistance Protein from Escherichia coli==
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PcoC is a soluble periplasmic protein encoded by the plasmid-born pco, copper resistance operon of Escherichia coli. Like PcoA, a multicopper, oxidase encoded in the same locus and its chromosomal homolog CueO, PcoC, contains unusual methionine rich sequences. Although essential for copper, resistance, the functions of PcoC, PcoA, and their conserved, methionine-rich sequences are not known. Similar methionine motifs, observed in eukaryotic copper transporters have been proposed to bind, copper, but there are no precedents for such metal binding sites in, structurally characterized proteins. The high-resolution structures of apo, PcoC, determined for both the native and selenomethionine-containing, proteins, reveal a seven-stranded beta barrel with the methionines, unexpectedly housed on a solvent-exposed loop. Several potential, metal-binding sites can be discerned by comparing the structures to, spectroscopic data reported for copper-loaded PcoC. In the native, structure, the methionine loop interacts with the same loop on a second, molecule in the asymmetric unit. In the selenomethionine structure, the, methionine loops are more exposed, forming hydrophobic patches on the, protein surface. These two arrangements suggest that the methionine motifs, might function in protein-protein interactions between PcoC molecules or, with other methionine-rich proteins such as PcoA. Analytical, ultracentrifugation data indicate that a weak monomer-dimer equilibrium, exists in solution for the apo protein. Dimerization is significantly, enhanced upon binding Cu(I) with a measured delta(deltaG degrees )&lt;or=-8.0, kJ/mole, suggesting that copper might bind at the dimer interface.
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<StructureSection load='1lyq' size='340' side='right'caption='[[1lyq]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1lyq]] is a 2 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=1LYQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LYQ FirstGlance]. <br>
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1LYQ 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 GOL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LYQ OCA].
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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]] 1.5&#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=GOL:GLYCEROL'>GOL</scene></td></tr>
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==Reference==
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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=1lyq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lyq OCA], [https://pdbe.org/1lyq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lyq RCSB], [https://www.ebi.ac.uk/pdbsum/1lyq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lyq ProSAT]</span></td></tr>
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Crystal structure and dimerization equilibria of PcoC, a methionine-rich copper resistance protein from Escherichia coli., Wernimont AK, Huffman DL, Finney LA, Demeler B, O'Halloran TV, Rosenzweig AC, J Biol Inorg Chem. 2003 Jan;8(1-2):185-94. Epub 2002 Sep 27. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12459914 12459914]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PCOC_ECOLX PCOC_ECOLX] Required for the copper-inducible expression of copper resistance.
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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/ly/1lyq_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=1lyq ConSurf].
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<div style="clear:both"></div>
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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: Demeler, B.]]
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[[Category: Demeler B]]
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[[Category: Finney, L.A.]]
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[[Category: Finney LA]]
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[[Category: Halloran, T.V.O.]]
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[[Category: Huffman DL]]
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[[Category: Huffman, D.L.]]
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[[Category: O'Halloran TV]]
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[[Category: Rosenzweig, A.C.]]
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[[Category: Rosenzweig AC]]
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[[Category: Wernimont, A.K.]]
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[[Category: Wernimont AK]]
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[[Category: GOL]]
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[[Category: beta barrel]]
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[[Category: ig domain]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:59:43 2007''
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Current revision

Crystal Structure of PcoC, a Methionine Rich Copper Resistance Protein from Escherichia coli

PDB ID 1lyq

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