6nfr: Difference between revisions
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==CopC from Pseudomonas fluorescens== | |||
<StructureSection load='6nfr' size='340' side='right'caption='[[6nfr]], [[Resolution|resolution]] 1.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6nfr]] is a 1 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=6NFR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6NFR 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]] 1Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=6nfr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nfr OCA], [https://pdbe.org/6nfr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6nfr RCSB], [https://www.ebi.ac.uk/pdbsum/6nfr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6nfr 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Maher | <div class="pdbe-citations 6nfr" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Pseudomonas fluorescens]] | |||
[[Category: Maher MJ]] | |||
Latest revision as of 06:52, 11 October 2023
CopC from Pseudomonas fluorescens
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