- Cryo-reconstructions of P22 polyheads suggest that phage assembly is nucleated by trimeric interactions among coat proteins.
- Parent KN, Sinkovits RS, Suhanovsky MM, Teschke CM, Egelman EH, Baker TS.SourceDepartment of Chemistry & Biochemistry, University of California, San Diego, La Jolla, CA, USA.
- Physical biology.Phys Biol.2010 Dec 9;7(4):045004. doi: 10.1088/1478-3975/7/4/045004.
- Bacteriophage P22 forms an isometric capsid during normal assembly, yet when the coat protein (CP) is altered at a single site, helical structures (polyheads) also form. The structures of three distinct polyheads obtained from F170L and F170A variants were determined by cryo-reconstruction methods.
- PMID 21149969
- Determinants of bacteriophage P22 polyhead formation: the role of coat protein flexibility in conformational switching.
- Suhanovsky MM, Parent KN, Dunn SE, Baker TS, Teschke CM.SourceDepartment of Molecular and Cell Biology, University of Connecticut, Storrs, CT, USA.
- Molecular microbiology.Mol Microbiol.2010 Sep;77(6):1568-82. doi: 10.1111/j.1365-2958.2010.07311.x. Epub 2010 Aug 18.
- We have investigated determinants of polyhead formation in bacteriophage P22 in order to understand the molecular mechanism by which coat protein assembly goes astray. Polyhead assembly is caused by amino acid substitutions in coat protein at position 170, which is located in the β-hinge. In vivo s
- PMID 20659287
- Polyhead formation in phage P22 pinpoints a region in coat protein required for conformational switching.
- Parent KN, Suhanovsky MM, Teschke CM.SourceDepartment of Molecular and Cell Biology, University of Connecticut, Storrs, CT, USA.
- Molecular microbiology.Mol Microbiol.2007 Sep;65(5):1300-10. Epub 2007 Aug 3.
- Eighteen single amino acid substitutions in phage P22 coat protein cause temperature-sensitive folding defects (tsf). Three intragenic global suppressor (su) substitutions (D163G, T166I and F170L), localized to a flexible loop, rescue the folding of several tsf coat proteins. Here we investigate the
- PMID 17680786
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