View source for 7bk5


==PfCopC mutant - E27A==
<StructureSection load='7bk5' size='340' side='right'caption='[[7bk5]], [[Resolution|resolution]] 1.54&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7bk5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_fluorescens_SBW25 Pseudomonas fluorescens SBW25]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BK5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BK5 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]] 1.54&#8491;</td></tr>
<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=PO4:PHOSPHATE+ION'>PO4</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=7bk5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bk5 OCA], [https://pdbe.org/7bk5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bk5 RCSB], [https://www.ebi.ac.uk/pdbsum/7bk5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bk5 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 histidine brace (His-brace) is a copper-binding motif that is associated with both oxidative enzymes and proteinaceous copper chaperones. Here, we used biochemical and structural methods to characterize mutants of a His-brace-containing copper chaperone from Pseudomonas fluorescens (PfCopC). A total of 15 amino acid variants in primary and second-sphere residues were produced and characterized in terms of their copper binding and redox properties. PfCopC has a very high affinity for Cu(II) and also binds Cu(I). A high reorganization barrier likely prevents redox cycling and, thus, catalysis. In contrast, mutations in the conserved second-sphere Glu27 enable slow oxidation of ascorbate. The crystal structure of the variant E27A confirmed copper binding at the His-brace. Unexpectedly, Asp83 at the equatorial position was shown to be indispensable for Cu(II) binding in the His-brace of PfCopC. A PfCopC mutant that was designed to mimic the His-brace from lytic polysaccharide monooxygenase-like family X325 did not bind Cu(II), but was still able to bind Cu(I). These results highlight the importance of the proteinaceous environment around the copper His-brace for reactivity and, thus, the difference between enzyme and chaperone.

Copper binding and reactivity at the histidine brace motif: insights from mutational analysis of the Pseudomonas fluorescens copper chaperone CopC.,Ipsen JO, Hernandez-Rollan C, Muderspach SJ, Brander S, Bertelsen AB, Jensen PE, Norholm MHH, Lo Leggio L, Johansen KS FEBS Lett. 2021 Jun;595(12):1708-1720. doi: 10.1002/1873-3468.14092. Epub 2021, May 14. PMID:33896006<ref>PMID:33896006</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7bk5" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas fluorescens SBW25]]
[[Category: Bertelsen AB]]
[[Category: Ipsen J]]
[[Category: Johansen KS]]
[[Category: Lo Leggio L]]
[[Category: Muderspach SJ]]
[[Category: Norholm MHH]]
[[Category: Rollan CH]]