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6nfr
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==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. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6NFR FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6nfr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nfr OCA], [http://pdbe.org/6nfr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6nfr RCSB], [http://www.ebi.ac.uk/pdbsum/6nfr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6nfr ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <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, M | + | <div class="pdbe-citations 6nfr" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Maher, M J]] | ||
| + | [[Category: Copc]] | ||
| + | [[Category: Copper binding]] | ||
| + | [[Category: Metal binding protein]] | ||
| + | [[Category: Metallochaperone]] | ||
Revision as of 07:00, 24 April 2019
CopC from Pseudomonas fluorescens
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