6wz7: Difference between revisions
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<StructureSection load='6wz7' size='340' side='right'caption='[[6wz7]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='6wz7' size='340' side='right'caption='[[6wz7]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'> | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6WZ7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6WZ7 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6wz7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wz7 OCA], [https://pdbe.org/6wz7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6wz7 RCSB], [https://www.ebi.ac.uk/pdbsum/6wz7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6wz7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 6wz7" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6wz7" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Cytochrome C 3D structures|Cytochrome C 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Kakkis | [[Category: Kakkis A]] | ||
[[Category: Tezcan | [[Category: Tezcan FA]] | ||
Latest revision as of 12:59, 25 December 2024
Mn-bound structure of a TriCyt3 variantMn-bound structure of a TriCyt3 variant
Structural highlights
Publication Abstract from PubMed<div class="abstract"> <div><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);">To mimic a hypothetical pathway for protein evolution, we previously developed a design strategy (Metal-Templated Interface Redesign), in which a monomeric protein (cytochrome <i>cb<sub>5</sub></i><sub>62&l t;/sub>) 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 <i>cb</i><sub>562</sub> surf ace can drastically alter the outcome of metal-directed oligomerization to yield a new trimeric architecture, (TriCyt1)<sub>3</sub>, featuring an unusual hexa-histidine coordination motif. Through computational and rational redesign, this nascent trimer is converted into second and third-generation variants (TriCyt2)<sub>3</sub> and (TriCyt3)<sub>3</sub> 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, rivaling those of the strongest Mn(II)-binding protein, calprotectin. <span lang="EN-GB" style="color: red;"><o:p></o:p></span></p> </div> </div>. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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