6nfs: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

~~The entry~~ 6nfs is ~~ON HOLD until Paper~~ Publication

==CopC from Pseudomonas fluorescens==

== Structural highlights ==

<table><tr><td colspan='2'>[[6nfs]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NFS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6NFS FirstGlance]. <br>

</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=6nfs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nfs OCA], [http://pdbe.org/6nfs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6nfs RCSB], [http://www.ebi.ac.uk/pdbsum/6nfs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6nfs ProSAT]</span></td></tr>

</table>

== 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.

~~Authors~~: ~~Maher, M~~.J.

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>

~~Description~~: ~~CopC from Pseudomonas fluorescens~~

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

[[Category: ~~Unreleased~~ Structures]]

</div>

[[Category: Maher, M.J]]

== References ==

__TOC__

</StructureSection>

[[Category: Large Structures]]

[[Category: Maher, M J]]

[[Category: Copc]]

[[Category: Copper binding]]

[[Category: Metal binding protein]]

[[Category: Metallochaperone]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6nfs is ON HOLD  until Paper Publication
+==CopC from Pseudomonas fluorescens==
+<StructureSection load='6nfs' size='340' side='right'caption='[[6nfs]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6nfs]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NFS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6NFS FirstGlance]. <br>
+</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=6nfs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nfs OCA], [http://pdbe.org/6nfs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6nfs RCSB], [http://www.ebi.ac.uk/pdbsum/6nfs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6nfs 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.
-Authors: Maher, M.J.
+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>
-Description: CopC from Pseudomonas fluorescens
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Maher, M.J]]
+<div class="pdbe-citations 6nfs" 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]]