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| | <StructureSection load='6x0q' size='340' side='right'caption='[[6x0q]], [[Resolution|resolution]] 3.00Å' scene=''> | | <StructureSection load='6x0q' size='340' side='right'caption='[[6x0q]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6x0q]] is a 17 chain structure with sequence from [http://en.wikipedia.org/wiki/Tmv Tmv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6X0Q OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6X0Q FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6x0q]] is a 17 chain structure with sequence from [https://en.wikipedia.org/wiki/Tmv Tmv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6X0Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6X0Q FirstGlance]. <br> |
| | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr> | | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr> |
| | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3kml|3kml]]</div></td></tr> | | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3kml|3kml]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=12243 TMV])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CP ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=12243 TMV])</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=6x0q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6x0q OCA], [http://pdbe.org/6x0q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6x0q RCSB], [http://www.ebi.ac.uk/pdbsum/6x0q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6x0q 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=6x0q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6x0q OCA], [https://pdbe.org/6x0q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6x0q RCSB], [https://www.ebi.ac.uk/pdbsum/6x0q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6x0q ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CAPSD_TMV CAPSD_TMV]] Capsid protein self-assembles to form rod-shaped virions about 18 nm in diameter with a central canal enclosing the viral genomic RNA. | + | [[https://www.uniprot.org/uniprot/CAPSD_TMV CAPSD_TMV]] Capsid protein self-assembles to form rod-shaped virions about 18 nm in diameter with a central canal enclosing the viral genomic RNA. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Structural highlights
Function
[CAPSD_TMV] Capsid protein self-assembles to form rod-shaped virions about 18 nm in diameter with a central canal enclosing the viral genomic RNA.
Publication Abstract from PubMed
Bioenergetic processes in nature have relied on networks of cofactors for harvesting, storing, and transforming the energy from sunlight into chemical bonds. Models mimicking the structural arrangement and functional crosstalk of the cofactor arrays are important tools to understand the basic science of natural systems and to provide guidance for non-natural functional biomaterials. Here, we report an artificial multiheme system based on a circular permutant of the tobacco mosaic virus coat protein (cpTMV). The double disk assembly of cpTMV presents a gap region sandwiched by the two C2-symmetrically related disks. Non-native bis-his coordination sites formed by the mutation of the residues in this gap region were computationally screened and experimentally tested. A cpTMV mutant Q101H was identified to create a circular assembly of 17 protein-embedded hemes. Biophysical characterization using X-ray crystallography, cyclic voltammetry, and electron paramagnetic resonance (EPR) suggested both structural and functional similarity to natural multiheme cytochrome c proteins. This protein framework offers many further engineering opportunities for tuning the redox properties of the cofactors and incorporating non-native components bearing varied porphyrin structures and metal centers. Emulating the electron transfer pathways in nature using a tunable artificial system can contribute to the development of photocatalytic materials and bioelectronics.
Protein-Embedded Metalloporphyrin Arrays Templated by Circularly Permuted Tobacco Mosaic Virus Coat Proteins.,Dai J, Knott GJ, Fu W, Lin TW, Furst AL, Britt RD, Francis MB ACS Nano. 2020 Dec 7. doi: 10.1021/acsnano.0c07165. PMID:33285072[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Dai J, Knott GJ, Fu W, Lin TW, Furst AL, Britt RD, Francis MB. Protein-Embedded Metalloporphyrin Arrays Templated by Circularly Permuted Tobacco Mosaic Virus Coat Proteins. ACS Nano. 2020 Dec 7. doi: 10.1021/acsnano.0c07165. PMID:33285072 doi:http://dx.doi.org/10.1021/acsnano.0c07165
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