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An Intramolecular Chaperone Inserted in Bacteriophage P22 Coat Protein Mediates Its Chaperonin-independent Folding
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 protei...
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| Główni autorzy: | , |
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| Format: | Artigo |
| Język: | Inglês |
| Wydane: |
American Society for Biochemistry and Molecular Biology
2013
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| Hasła przedmiotowe: | |
| Dostęp online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3837121/ https://ncbi.nlm.nih.gov/pubmed/24126914 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M113.515312 |
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