ArticleThe Journal of biological chemistry2013
An intramolecular chaperone inserted in bacteriophage P22 coat protein mediates its chaperonin-independent folding.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 16 citations in OpenAlex.
- 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
- The phage L capsid decoration protein has a novel OB-fold and an unusual capsid binding strategy.eLife · 2019Article
- Contributions of P2- and P22-like prophages to understanding the enormous diversity and abundance of tailed bacteriophages.Virology · 2016Article
- Article
- Contextual Role of a Salt Bridge in the Phage P22 Coat Protein I-Domain.The Journal of biological chemistry · 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
- NMR assignments for the insertion domain of bacteriophage CUS-3 coat protein.Biomolecular NMR assignments · 2015Article
- Nature's favorite building block: Deciphering folding and capsid assembly of proteins with the HK97-fold.Virology · 2015Review
- Domains of Pyrococcus furiosus L-asparaginase fold sequentially and assemble through strong intersubunit associative forces.Extremophiles : life under extreme conditions · 2015Article
- Article
- 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
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The bacteriophage P22 coat protein has the common HK97-like fold but with a genetically inserted domain (I-domain). The role of the I-domain, positioned at the outermost surface of the capsid, is unknown. We hypothesize that the I-domain may act as an intramolecular chaperone because the coat protein folds independently, and many folding mutants are localized to the I-domain. The function of the I-domain was investigated by generating the coat protein core without its I-domain and the isolated I-domain. The core coat protein shows a pronounced folding defect. The isolated I-domain folds autonomously and has a high thermodynamic stability and fast folding kinetics in the presence of a peptidyl prolyl isomerase. Thus, the I-domain provides thermodynamic stability to the full-length coat protein so that it can fold reasonably efficiently while still allowing the HK97-like core to retain the flexibility required for conformational switching during procapsid assembly and maturation.
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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.