View source for 6r01


==Streptomyces lividans Ccsp mutant - H107A/H111A==
<StructureSection load='6r01' size='340' side='right'caption='[[6r01]], [[Resolution|resolution]] 1.18&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6r01]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_lividans_1326 Streptomyces lividans 1326]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6R01 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6R01 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]] 1.18&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</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=6r01 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6r01 OCA], [https://pdbe.org/6r01 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6r01 RCSB], [https://www.ebi.ac.uk/pdbsum/6r01 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6r01 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9X8F4_STRCO Q9X8F4_STRCO] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The chemical basis for protecting organisms against the toxic effect imposed by excess cuprous ions is to constrain this through high-affinity binding sites that employ cuprous-thiolate coordination chemistries. In bacteria, a family of cysteine rich four helix-bundle proteins utilise thiolate chemistry to bind up to 80 cuprous ions. These proteins have been termed copper storage proteins (Csp). The present study investigates cuprous ion loading to the Csp from Streptomyces lividans (SlCsp) using a combination of X-ray crystallography, site-directed mutagenesis and stopped-flow reaction kinetics with either aquatic cuprous ions or a chelating donor. We illustrate that at low cuprous ion concentrations, copper is loaded exclusively into an outer core region of SlCsp via one end of the four helix-bundle, facilitated by a set of three histidine residues. X-ray crystallography reveals the existence of polynuclear cuprous-thiolate clusters culminating in the assembly of a tetranuclear [Cu4(mu2-S-Cys)4(Nudelta1-His)] cluster in the outer core. As more cuprous ions are loaded, the cysteine lined inner core of SlCsp fills with cuprous ions but in a fluxional and dynamic manner with no evidence for the assembly of further intermediate polynuclear cuprous-thiolate clusters as observed in the outer core. Using site-directed mutagenesis a key role for His107 in the efficient loading of cuprous ions from a donor is established. A model of copper loading to SlCsp is proposed and discussed.

A histidine residue and a tetranuclear cuprous-thiolate cluster dominate the copper loading landscape of a copper storage protein from Streptomyces lividans.,Straw ML, Hough MA, Wilson MT, Worrall JAR Chemistry. 2019 May 21. doi: 10.1002/chem.201901411. PMID:31111982<ref>PMID:31111982</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6r01" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces lividans 1326]]
[[Category: Hough MA]]
[[Category: Straw ML]]
[[Category: Worrall JA]]