This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
6x8x
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 6x8x is ON HOLD Authors: Tezcan, F.A., Kakkis, A. Description: Cu-bound structure of an engineered metal-dependent protein trimer, TriCyt1 [[Catego...) |
|||
| (4 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Cu-bound structure of an engineered metal-dependent protein trimer, TriCyt1== | |
| + | <StructureSection load='6x8x' size='340' side='right'caption='[[6x8x]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6x8x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6X8X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6X8X 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]] 2.505Å</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=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</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=6x8x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6x8x OCA], [https://pdbe.org/6x8x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6x8x RCSB], [https://www.ebi.ac.uk/pdbsum/6x8x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6x8x ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/C562_ECOLX C562_ECOLX] Electron-transport protein of unknown function. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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&nbsp;<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&nbsp;<i>cb</i><sub>562</sub>&nbsp;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>&nbsp;and (TriCyt3)<sub>3</sub>&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,&nbsp;&nbsp;rivaling those of the strongest Mn(II)-binding protein, calprotectin.&nbsp;<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<ref>PMID:32830423</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Kakkis | + | <div class="pdbe-citations 6x8x" style="background-color:#fffaf0;"></div> |
| - | [[Category: Tezcan | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia coli]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Kakkis A]] | ||
| + | [[Category: Tezcan FA]] | ||
Current revision
Cu-bound structure of an engineered metal-dependent protein trimer, TriCyt1
| |||||||||||
