View source for 6nfq


==CopC from Pseudomonas fluorescens==
<StructureSection load='6nfq' size='340' side='right'caption='[[6nfq]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6nfq]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_fluorescens Pseudomonas fluorescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NFQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6NFQ FirstGlance]. <br>
</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&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=YT3:YTTRIUM+(III)+ION'>YT3</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6nfq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nfq OCA], [https://pdbe.org/6nfq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6nfq RCSB], [https://www.ebi.ac.uk/pdbsum/6nfq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6nfq ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/C3JYL7_PSEFS C3JYL7_PSEFS] Involved in copper resistance.[RuleBase:RU369037]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The bacterial CopC family of proteins are periplasmic copper binding proteins that act in copper detoxification. These proteins contain Cu(I) and/or Cu(II) binding sites, with the family that binds Cu(II) only the most prevalent, based on sequence analyses. Here we present three crystal structures of the CopC protein from Pseudomonas fluorescens (Pf-CopC) that include the wild type protein bound to Cu(II) and two variant proteins, where Cu(II) coordinating ligands were mutated, in Cu-free states. We show that the Cu(II) atom in Pf-CopC is coordinated by two His residues, an Asp residue and the N-terminus of the protein (therefore a 3N+O site). This coordination structure is consistent with all structurally characterized proteins from the CopC family to date. Structural and sequence analyses of the CopC family allow a relationship between protein sequence and the Cu(II) binding affinity of these proteins to be proposed.

The crystal structure of the CopC protein from Pseudomonas fluorescens reveals amended classifications for the CopC protein family.,Udagedara SR, Wijekoon CJK, Xiao Z, Wedd AG, Maher MJ J Inorg Biochem. 2019 Mar 21;195:194-200. doi: 10.1016/j.jinorgbio.2019.03.007. PMID:30981030<ref>PMID:30981030</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6nfq" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas fluorescens]]
[[Category: Maher MJ]]