ArticleVirology2011
Bacteriophage P22 capsid size determination: roles for the coat protein telokin-like domain and the scaffolding protein amino-terminus.
Article in Virology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 28 citations in OpenAlex.
- Structural insights into scaffold-guided assembly of the Pseudomonas phage D3 capsid.Nature communications · 2025Article
- A structural dendrogram of the actinobacteriophage major capsid proteins provides important structural insights into the evolution of capsid stability.Structure (London, England : 1993) · 2023Article
- Applications of Charge Detection Mass Spectrometry in Molecular Biology and Biotechnology.Chemical reviews · 2022Review
- NMR Mapping of Disordered Segments from a Viral Scaffolding Protein Enclosed in a 23 MDa Procapsid.Biophysical journal · 2019Article
- Article
- The amazing HK97 fold: versatile results of modest differences.Current opinion in virology · 2019Review
- Conservation and Divergence of the I-Domain Inserted into the Ubiquitous HK97 Coat Protein Fold in P22-Like Bacteriophages.Journal of virology · 2019Article
- Coat Protein Mutations That Alter the Flux of Morphogenetic Intermediates through the ϕX174 Early Assembly Pathway.Journal of virology · 2017Article
- A viral scaffolding protein triggers portal ring oligomerization and incorporation during procapsid assembly.Science advances · 2017Article
- Acquiring Structural Information on Virus Particles with Charge Detection Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2016Article
- Mechanism of Protein Denaturation: Partial Unfolding of the P22 Coat Protein I-Domain by Urea Binding.Biophysical journal · 2015Article
- A Molecular Staple: D-Loops in the I Domain of Bacteriophage P22 Coat Protein Make Important Intercapsomer Contacts Required for Procapsid Assembly.Journal of virology · 2015Article
- Nature's favorite building block: Deciphering folding and capsid assembly of proteins with the HK97-fold.Virology · 2015Review
- Multiple functional roles of the accessory I-domain of bacteriophage P22 coat protein revealed by NMR structure and CryoEM modeling.Structure (London, England : 1993) · 2014Article
- Transient contacts on the exterior of the HK97 procapsid that are essential for capsid assembly.Journal of molecular biology · 2014Article
- Highly specific salt bridges govern bacteriophage P22 icosahedral capsid assembly: identification of the site in coat protein responsible for interaction with scaffolding protein.Journal of virology · 2014Article
- NMR assignments for the telokin-like domain of bacteriophage P22 coat protein.Biomolecular NMR assignments · 2013Article
- Unraveling the role of the C-terminal helix turn helix of the coat-binding domain of bacteriophage P22 scaffolding protein.The Journal of biological chemistry · 2012Article
- The energetic contributions of scaffolding and coat proteins to the assembly of bacteriophage procapsids.Virology · 2012Article
- Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Assembly of icosahedral capsids of proper size and symmetry is not understood. Residue F170 in bacteriophage P22 coat protein is critical for conformational switching during assembly. Substitutions at this site cause assembly of tubes of hexamerically arranged coat protein. Intragenic suppressors of the ts phenotype of F170A and F170K coat protein mutants were isolated. Suppressors were repeatedly found in the coat protein telokin-like domain at position 285, which caused coat protein to assemble into petite procapsids and capsids. Petite capsid assembly strongly correlated to the side chain volume of the substituted amino acid. We hypothesize that larger side chains at position 285 torque the telokin-like domain, changing flexibility of the subunit and intercapsomer contacts. Thus, a single amino acid substitution in coat protein is sufficient to change capsid size. In addition, the products of assembly of the variant coat proteins were affected by the size of the internal scaffolding protein.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.