Abstract
The P22 phage system is an intensely studied model system. Studies have ranged from biochemical analysis of basic life processes to the use of this phage for phage therapy. The phage tailspike protein (TSP) has itself been the subject of intensive studies over the past fifty years. The P22 TSP is essential for initiation of the infection process and instrumental as the last protein assembled onto the phage particle structure to complete its assembly. It has also been the subject for many structural studies including cryoelectron microscopic analysis and photophysical studies. It has been a model for in vivo and in vitro protein folding including analysis using P22 TSP temperature-sensitive for folding mutations (tsf). Recently the structure and function of the N-terminal domain (NTD), including some aspects of the structural stability of the P22 TSP NTD (aa1-aa108), are being genetically dissected. This report strongly supports the notion that two amino acids, not localized to the internal NTD dome stem, are important in the structural stability of the P22 TSP NTD.
Highlights
The bacteriophage P22 is a well-studied phage system as well as being an intensely used model for a number of life processes and proteins
The P22 tailspike protein (TSP) N-terminal domain (NTD) binds to the crevice formed between the GP4 and GP10 viral structural proteins while a crevice formed by two sets of peptide ridges, located in the β-helix domain is responsible for host cell LPS binding and hydrolysis [14] [15]
Mutations in the DNA Sequence Corresponding to the N-Terminal Domain
Summary
The bacteriophage (phage) P22 is a well-studied phage system as well as being an intensely used model for a number of life processes and proteins. It is the last protein to be added in the phage assembly pathway to yield a completed infectious particle [7] [8]. This last assembly step, when done in vitro, is called tailing. The P22 TSP NTD binds to the crevice formed between the GP4 and GP10 viral structural proteins while a crevice formed by two sets of peptide ridges, located in the β-helix domain is responsible for host cell LPS binding and hydrolysis [14] [15]. Recent studies on the structure and function of the P22 TSP NTD have found amino acids, located within the interior of the NTD dome, are involved in the stability of the domain structure [16]. This Short Communication presents preliminary studies strongly suggesting two amino acids, which are not localized in the stem region, and may be important determinants in the overall stability of the P22 TSP NTD
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