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5icu

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<StructureSection load='5icu' size='340' side='right'caption='[[5icu]], [[Resolution|resolution]] 1.46&Aring;' scene=''>
<StructureSection load='5icu' size='340' side='right'caption='[[5icu]], [[Resolution|resolution]] 1.46&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5icu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Methylosinus_trichosporium_ob3b Methylosinus trichosporium ob3b]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ICU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ICU FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5icu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methylosinus_trichosporium_OB3b Methylosinus trichosporium OB3b]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ICU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ICU FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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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]] 1.46&#8491;</td></tr>
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<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=5icu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5icu OCA], [http://pdbe.org/5icu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5icu RCSB], [http://www.ebi.ac.uk/pdbsum/5icu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5icu ProSAT]</span></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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=5icu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5icu OCA], [https://pdbe.org/5icu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5icu RCSB], [https://www.ebi.ac.uk/pdbsum/5icu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5icu ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/A0A158RFT6_METTR A0A158RFT6_METTR]
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The CopC proteins are periplasmic copper binding proteins believed to play a role in bacterial copper homeostasis. Previous studies have focused on CopCs that are part of seven-protein Cop or Pco systems involved in copper resistance. These canonical CopCs contain distinct Cu(I) and Cu(II) binding sites. Mounting evidence suggests that CopCs are more widely distributed, often present only with the CopD inner membrane protein, frequently as a fusion protein, and that the CopC and CopD proteins together function in the uptake of copper to the cytoplasm. In the methanotroph Methylosinus trichosporium OB3b, genes encoding a CopCD pair are located adjacent to the particulate methane monooxygenase (pMMO) operon. The CopC from this organism (Mst-CopC) was expressed, purified, and structurally characterized. The 1.46 A resolution crystal structure of Mst-CopC reveals a single Cu(II) binding site with coordination somewhat different from that in canonical CopCs, and the absence of a Cu(I) binding site. Extensive bioinformatic analyses indicate that the majority of CopCs in fact contain only a Cu(II) site, with just 10% of sequences corresponding to the canonical two-site CopC. Accordingly, a new classification scheme for CopCs was developed, and detailed analyses of the sequences and their genomic neighborhoods reveal new proteins potentially involved in copper homeostasis, providing a framework for expanded models of CopCD function.
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The CopC Family: Structural and Bioinformatic Insights into a Diverse Group of Periplasmic Copper Binding Proteins.,Lawton TJ, Kenney GE, Hurley JD, Rosenzweig AC Biochemistry. 2016 Apr 19;55(15):2278-90. doi: 10.1021/acs.biochem.6b00175. Epub , 2016 Apr 6. PMID:27010565<ref>PMID:27010565</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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<div class="pdbe-citations 5icu" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Methylosinus trichosporium ob3b]]
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[[Category: Methylosinus trichosporium OB3b]]
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[[Category: Hurley, J D]]
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[[Category: Hurley JD]]
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[[Category: Lawton, T J]]
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[[Category: Lawton TJ]]
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[[Category: Rosenzweig, A C]]
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[[Category: Rosenzweig AC]]
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[[Category: Chaperone]]
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[[Category: Copc]]
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[[Category: Cupredoxin]]
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[[Category: Metal homeostasis]]
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[[Category: Pcoc]]
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Current revision

The crystal structure of CopC from Methylosinus trichosporium OB3b

PDB ID 5icu

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