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Steinbacher, S., Miller, S., Baxa, U., Budisa, N., Weintraub, A., Seckler, R. and Huber, R. (1997) Phage P22 Tailspike Protein: Crystal Structure of the Head-Binding Domain at 2.3 A, Fully Refined Structure of the Endorhamnosidase at 1.56 A Resolution, and the Molecular Basis of O-Antigen Recognition and Cleavage. Journal of Molecular Biology, 267, 865-880. http://dx.doi.org/10.1006/jmbi.1997.0922

has been cited by the following article:

• TITLE: Non-Stem Amino Acids Are Involved in the Phage P22 TSP NTD Stability

  AUTHORS: Karthikeya Venkatesan, Jeremie Williams, Robert Villafane

  KEYWORDS: N-Terminal Domain (NTD), P22 Phage, Tailspike Protein (TSP), Mutagenesis, Structural Stability

  JOURNAL NAME: Advances in Microbiology, Vol.4 No.9, July 24, 2014

  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.