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| | <StructureSection load='6x7e' size='340' side='right'caption='[[6x7e]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='6x7e' size='340' side='right'caption='[[6x7e]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6x7e]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6X7E OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6X7E FirstGlance]. <br> | + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6X7E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6X7E FirstGlance]. <br> |
| - | </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=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9987Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cybC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6x7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6x7e OCA], [http://pdbe.org/6x7e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6x7e RCSB], [http://www.ebi.ac.uk/pdbsum/6x7e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6x7e ProSAT]</span></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=6x7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6x7e OCA], [https://pdbe.org/6x7e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6x7e RCSB], [https://www.ebi.ac.uk/pdbsum/6x7e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6x7e ProSAT]</span></td></tr> |
| | </table> | | </table> |
| - | == Function == | |
| - | [[http://www.uniprot.org/uniprot/C562_ECOLX C562_ECOLX]] Electron-transport protein of unknown function. | |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kakkis, A]] | + | [[Category: Kakkis A]] |
| - | [[Category: Tezcan, F A]] | + | [[Category: Tezcan FA]] |
| - | [[Category: Four-helix bundle]]
| + | |
| - | [[Category: Metal binding protein]]
| + | |
| - | [[Category: Metalloprotein trimer]]
| + | |
| 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.
References
- ↑ Tezcan FA, Kakkis A, Gagnon D, Esselborn J, Britt RD. Metal-Templated Design of Chemically Switchable Protein Assemblies with High-Affinity Coordination Sites. Angew Chem Int Ed Engl. 2020 Aug 23. doi: 10.1002/anie.202009226. PMID:32830423 doi:http://dx.doi.org/10.1002/anie.202009226
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