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.
Highlights
The bacteriophage P22 coat protein has an HK97-like fold with an additional, genetically inserted domain
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
There is a balance between the stability of the monomeric coat protein and the structural flexibility required for conformational switching during assembly and maturation
Summary
The bacteriophage P22 coat protein has an HK97-like fold with an additional, genetically inserted domain. Results: The insertion domain provides thermodynamic stability to the full-length coat protein. The bacteriophage P22 coat protein has the common HK97like fold but with a genetically inserted domain (I-domain). 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. The coat proteins of viruses with icosahedral symmetry must retain sufficient flexibility for assembly and maturation. Ing chaperonins for the proper folding of their viral coat proteins One member of this group, bacteriophage P22, is an exception to this generality. Characterization of the isolated I-domain and the coat protein core was performed to elucidate the role of this domain
Sign-in/Register to view highlights & summary Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
