6x0r: Difference between revisions
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<StructureSection load='6x0r' size='340' side='right'caption='[[6x0r]], [[Resolution|resolution]] 3.00Å' scene=''> | <StructureSection load='6x0r' size='340' side='right'caption='[[6x0r]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6x0r]] is a 17 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[6x0r]] is a 17 chain structure with sequence from [https://en.wikipedia.org/wiki/Tobacco_mosaic_virus_(vulgare) Tobacco mosaic virus (vulgare)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6X0R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6X0R FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</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=6x0r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6x0r OCA], [https://pdbe.org/6x0r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6x0r RCSB], [https://www.ebi.ac.uk/pdbsum/6x0r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6x0r 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=6x0r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6x0r OCA], [https://pdbe.org/6x0r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6x0r RCSB], [https://www.ebi.ac.uk/pdbsum/6x0r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6x0r ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[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 == | ||
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</div> | </div> | ||
<div class="pdbe-citations 6x0r" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6x0r" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Tobacco Mosaic Virus|Tobacco Mosaic Virus]] | |||
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Dai J]] | |||
[[Category: Dai | [[Category: Francis MB]] | ||
[[Category: Francis | [[Category: Knott GJ]] | ||
[[Category: Knott | |||
Latest revision as of 17:40, 18 October 2023
A Circular Permutant of the Tobacco Mosaic Virus (TMV) mutant Q101HA Circular Permutant of the Tobacco Mosaic Virus (TMV) mutant Q101H
Structural highlights
FunctionCAPSD_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 PubMedBioenergetic 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. See AlsoReferences
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