View source for 6wz3


==Cu-bound structure of the engineered protein trimer, TriCyt3==
<StructureSection load='6wz3' size='340' side='right'caption='[[6wz3]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6WZ3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6WZ3 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]] 1.8&#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=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=6wz3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wz3 OCA], [https://pdbe.org/6wz3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6wz3 RCSB], [https://www.ebi.ac.uk/pdbsum/6wz3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6wz3 ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
&lt;div class="abstract"&gt; &lt;div&gt;&lt;p class="Abstract" style="margin: 0in 0in 0.25in; text-align: justify; line-height: 11.25pt; font-size: 8pt; font-family: Arial, sans-serif; caret-color: rgb(0, 0, 0); color: rgb(0, 0, 0);"&gt;To mimic a hypothetical pathway for protein evolution, we previously developed a design strategy (Metal-Templated Interface Redesign), in which a monomeric protein (cytochrome&amp;nbsp;&lt;i&gt;cb&lt;sub&gt;5&lt;/sub&gt;&lt;/i&gt;&lt;sub&gt;62&amp;l t;/sub&gt;) was tailored for metal-mediated self-assembly, followed by the re-design of the resulting oligomers for enhanced stability and metal-based functions. Here we show that a single hydrophobic mutation on the cytochrome&amp;nbsp;&lt;i&gt;cb&lt;/i&gt;&lt;sub&gt;562&lt;/sub&gt;&amp;nbsp;surf ace can drastically alter the outcome of metal-directed oligomerization to yield a new trimeric architecture, (TriCyt1)&lt;sub&gt;3&lt;/sub&gt;, featuring an unusual hexa-histidine coordination motif. Through computational and rational redesign, this nascent trimer is converted into second and third-generation variants (TriCyt2)&lt;sub&gt;3&lt;/sub&gt;&amp;nbsp;and (TriCyt3)&lt;sub&gt;3&lt;/sub&gt;&amp;nbsp;with increased structural stability and preorganization for metal coordination. The three TriCyt variants combined furnish a unique design platform to a) provide tunable coupling between protein quaternary structure and metal coordination, b) enable the construction of metal/pH-switchable protein oligomerization motifs, and c) generate a robust metal coordination site that can accommodate all mid-to-late first-row transition metal ions with high affinity, including Mn(II) with nanomolar dissociation constants,&amp;nbsp;&amp;nbsp;rivaling those of the strongest Mn(II)-binding protein, calprotectin.&amp;nbsp;&lt;span lang="EN-GB" style="color: red;"&gt;&lt;o:p&gt;&lt;/o:p&gt;&lt;/span&gt;&lt;/p&gt; &lt;/div&gt; &lt;/div&gt;.

Metal-Templated Design of Chemically Switchable Protein Assemblies with High-Affinity Coordination Sites.,Tezcan FA, Kakkis A, Gagnon D, Esselborn J, Britt RD Angew Chem Int Ed Engl. 2020 Aug 23. doi: 10.1002/anie.202009226. PMID:32830423<ref>PMID:32830423</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6wz3" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Kakkis A]]
[[Category: Tezcan FA]]