9oh5

From Proteopedia

(Difference between revisions)

Current revision

Cryo-EM structure of the assembled MS2 CPM58 VLP

Structural highlights

9oh5 is a 2 chain structure with sequence from Escherichia phage MS2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 2.62Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CAPSD_BPMS2 Self-assembles to form the T=3 icosahedral virus shell that protects the viral nucleic acid. Acts as a translational repressor by binding with high specificity to a single stem-loop structure in the genomic RNA that contains the initiation codon of the gene for the viral replicase. Involved in virus assembly through the interaction between a capsid protein dimer and the multiple packaging signals present in the RNA genome.^[1] ^[2] ^[3] ^[4] ^[5] ^[6]

Publication Abstract from PubMed

Virus-like particles (VLPs) are self-assembling nanoparticles derived from viruses with the potential as scaffolds for myriad applications. They are also excellent testbeds for engineering protein superstructures. Engineers often employ techniques such as amino acid substitutions and insertions/deletions. Yet evolution also utilizes circular permutation, a powerful natural strategy that has not been fully explored in engineering self-assembling protein nanoparticles. Here, we demonstrate this technique using the MS2 VLP as a model self-assembling proteinaceous nanoparticle. We constructed a comprehensive circular permutation library of the fused MS2 coat protein dimer construct. The strategy revealed terminal locations, validated via cryo-electron microscopy, that enabled C-terminal peptide tagging and led to a protein encapsulation strategy via covalent bonding - a feature the native coat protein does not permit. Our systematic study demonstrates the power of circular permutation for engineering features as well as quantitatively and systematically exploring VLP structural determinants.

Synthetic Rewiring of Virus-like Particles via Circular Permutation Enables Modular Peptide Display and Protein Encapsulation.,Liang S, Butaney K, de Castro Assumpcao D, Jung J, Kennedy NW, Tullman-Ercek D ACS Nano. 2025 Oct 29. doi: 10.1021/acsnano.5c12293. PMID:41159643^[7]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Horn WT, Tars K, Grahn E, Helgstrand C, Baron AJ, Lago H, Adams CJ, Peabody DS, Phillips SE, Stonehouse NJ, Liljas L, Stockley PG. Structural basis of RNA binding discrimination between bacteriophages Qbeta and MS2. Structure. 2006 Mar;14(3):487-95. PMID:16531233 doi:http://dx.doi.org/10.1016/j.str.2005.12.006
↑ Plevka P, Tars K, Liljas L. Crystal packing of a bacteriophage MS2 coat protein mutant corresponds to octahedral particles. Protein Sci. 2008 Oct;17(10):1731-9. Epub 2008 Jul 28. PMID:18662904 doi:10.1110/ps.036905.108
↑ Rolfsson O, Middleton S, Manfield IW, White SJ, Fan B, Vaughan R, Ranson NA, Dykeman E, Twarock R, Ford J, Kao CC, Stockley PG. Direct Evidence for Packaging Signal-Mediated Assembly of Bacteriophage MS2. J Mol Biol. 2016 Jan 29;428(2 Pt B):431-48. doi: 10.1016/j.jmb.2015.11.014. Epub , 2015 Dec 1. PMID:26608810 doi:http://dx.doi.org/10.1016/j.jmb.2015.11.014
↑ Golmohammadi R, Valegard K, Fridborg K, Liljas L. The refined structure of bacteriophage MS2 at 2.8 A resolution. J Mol Biol. 1993 Dec 5;234(3):620-39. PMID:8254664 doi:http://dx.doi.org/10.1006/jmbi.1993.1616
↑ Valegard K, Murray JB, Stonehouse NJ, van den Worm S, Stockley PG, Liljas L. The three-dimensional structures of two complexes between recombinant MS2 capsids and RNA operator fragments reveal sequence-specific protein-RNA interactions. J Mol Biol. 1997 Aug 1;270(5):724-38. PMID:9245600 doi:http://dx.doi.org/10.1006/jmbi.1997.1144
↑ van den Worm SH, Stonehouse NJ, Valegard K, Murray JB, Walton C, Fridborg K, Stockley PG, Liljas L. Crystal structures of MS2 coat protein mutants in complex with wild-type RNA operator fragments. Nucleic Acids Res. 1998 Mar 1;26(5):1345-51. PMID:9469847
↑ Liang S, Butaney K, de Castro Assumpção D, Jung J, Kennedy NW, Tullman-Ercek D. Synthetic Rewiring of Virus-like Particles via Circular Permutation Enables Modular Peptide Display and Protein Encapsulation. ACS Nano. 2025 Oct 29. PMID:41159643 doi:10.1021/acsnano.5c12293

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/9oh5"

Categories: Escherichia phage MS2 | Large Structures | Jung J | Liang S | Tullman-Ercek D

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 9oh5 is ON HOLD  until 2027-05-02
+==Cryo-EM structure of the assembled MS2 CPM58 VLP==
+<StructureSection load='9oh5' size='340' side='right'caption='[[9oh5]], [[Resolution|resolution]] 2.62&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[9oh5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_phage_MS2 Escherichia phage MS2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9OH5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9OH5 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.62&#8491;</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=9oh5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9oh5 OCA], [https://pdbe.org/9oh5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9oh5 RCSB], [https://www.ebi.ac.uk/pdbsum/9oh5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9oh5 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CAPSD_BPMS2 CAPSD_BPMS2] Self-assembles to form the T=3 icosahedral virus shell that protects the viral nucleic acid. Acts as a translational repressor by binding with high specificity to a single stem-loop structure in the genomic RNA that contains the initiation codon of the gene for the viral replicase. Involved in virus assembly through the interaction between a capsid protein dimer and the multiple packaging signals present in the RNA genome.<ref>PMID:16531233</ref> <ref>PMID:18662904</ref> <ref>PMID:26608810</ref> <ref>PMID:8254664</ref> <ref>PMID:9245600</ref> <ref>PMID:9469847</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Virus-like particles (VLPs) are self-assembling nanoparticles derived from viruses with the potential as scaffolds for myriad applications. They are also excellent testbeds for engineering protein superstructures. Engineers often employ techniques such as amino acid substitutions and insertions/deletions. Yet evolution also utilizes circular permutation, a powerful natural strategy that has not been fully explored in engineering self-assembling protein nanoparticles. Here, we demonstrate this technique using the MS2 VLP as a model self-assembling proteinaceous nanoparticle. We constructed a comprehensive circular permutation library of the fused MS2 coat protein dimer construct. The strategy revealed terminal locations, validated via cryo-electron microscopy, that enabled C-terminal peptide tagging and led to a protein encapsulation strategy via covalent bonding - a feature the native coat protein does not permit. Our systematic study demonstrates the power of circular permutation for engineering features as well as quantitatively and systematically exploring VLP structural determinants.
-Authors:
+Synthetic Rewiring of Virus-like Particles via Circular Permutation Enables Modular Peptide Display and Protein Encapsulation.,Liang S, Butaney K, de Castro Assumpcao D, Jung J, Kennedy NW, Tullman-Ercek D ACS Nano. 2025 Oct 29. doi: 10.1021/acsnano.5c12293. PMID:41159643<ref>PMID:41159643</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 9oh5" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Escherichia phage MS2]]
+[[Category: Large Structures]]
+[[Category: Jung J]]
+[[Category: Liang S]]
+[[Category: Tullman-Ercek D]]

9oh5

From Proteopedia

Current revision

Cryo-EM structure of the assembled MS2 CPM58 VLP

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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