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Small crosslink may stabilize P22 tail protein at N‐terminus
Author(s) -
Palmer Chris,
Johnson Sam,
Dean Dexter,
Villafane Robert
Publication year - 2013
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.27.1_supplement.1004.12
Subject(s) - amino acid , mutagenesis , dome (geology) , chemistry , c terminus , domain (mathematical analysis) , amino acid residue , molecular dynamics , n terminus , peptide sequence , biophysics , biochemistry , stereochemistry , biology , mutation , computational chemistry , gene , paleontology , mathematical analysis , mathematics
The goal of this study is to determine if a 13 amino acid sequence (aa) is responsible for maintaining the structural stability of the N‐terminus domain of the P22 tailspike protein (TSP). The phage P22 TSP functions as a homotrimer and contains two major structural domains. The first domain consists of 108aa and functions as a homotrimer, taking on the form of a “dome”. Each of the three identical polypeptide chains contributes 23aa at the center of the dome which has been termed the “stem”. This short stem starts with aa23 at the dome top and travels through the dome interior to aa1 the dome bottom. We have determined through a molecular visualization program that the first 13aa of the stem are located at the adjacent chain. They form a hydrophobic interaction and may crosslink adjacent chains providing the rational for structural stability at the NTD. We have changed two out of the four stem hydrophobic residues to aspartic acid by QuikChange Mutagenesis and have determined by a petri plate assay (the Berget Plate Assay) that V9D change causes a change that destroys NTD function. Biochemical studies are continuing to determine the mechanism for this reaction and to study the remaining three amino acids.