6F7K

Crystal structure of Dettilon tailspike protein (gp208)

Summary for 6F7K

• Entry DOI: 10.2210/pdb6f7k/pdb
• Related: 6F7D
• Descriptor: Tailspike, alpha-D-galactopyranose-(1-6)-beta-D-mannopyranose-(1-4)-alpha-L-rhamnopyranose-(1-3)-alpha-D-galactopyranose-(1-6)-beta-D-mannopyranose-(1-4)-alpha-L-rhamnopyranose, alpha-D-galactopyranose-(1-6)-beta-D-mannopyranose-(1-4)-alpha-L-rhamnopyranose-(1-3)-alpha-D-galactopyranose, ... (6 entities in total)
• Functional Keywords: det7, dettilon, tailspike, myovirus, sugar binding protein
• Biological source: Salmonella phage Det7
• Total number of polymer chains: 6
• Total formula weight: 354314.49

Authors

Roske, Y.,Heinemann, U. (deposition date: 2017-12-11, release date: 2018-12-19, Last modification date: 2024-01-17)

Primary citation

Broeker, N.K.,Roske, Y.,Valleriani, A.,Stephan, M.S.,Andres, D.,Koetz, J.,Heinemann, U.,Barbirz, S.
Time-resolved DNA release from an O-antigen-specificSalmonellabacteriophage with a contractile tail.
J.Biol.Chem., 294:11751-11761, 2019

PubMed Abstract: Myoviruses, bacteriophages with T4-like architecture, must contract their tails prior to DNA release. However, quantitative kinetic data on myovirus particle opening are lacking, although they are promising tools in bacteriophage-based antimicrobial strategies directed against Gram-negative hosts. For the first time, we show time-resolved DNA ejection from a bacteriophage with a contractile tail, the multi-O-antigen-specific myovirus Det7. DNA release from Det7 was triggered by lipopolysaccharide (LPS) O-antigen receptors and notably slower than in noncontractile-tailed siphoviruses. Det7 showed two individual kinetic steps for tail contraction and particle opening. Our studies showed that highly specialized tailspike proteins (TSPs) are necessary to attach the particle to LPS. A P22-like TSP confers specificity for the Typhimurium O-antigen. Moreover, crystal structure analysis at 1.63 Å resolution confirmed that Det7 recognized the Anatum O-antigen via an ϵ15-like TSP, DettilonTSP. DNA ejection triggered by LPS from either host showed similar velocities, so particle opening is thus a process independent of O-antigen composition and the recognizing TSP. In Det7, at permissive temperatures TSPs mediate O-antigen cleavage and couple cell surface binding with DNA ejection, but no irreversible adsorption occurred at low temperatures. This finding was in contrast to short-tailed podoviruses, illustrating that tailed phages use common particle-opening mechanisms but have specialized into different infection niches.

PubMed: 31189652
DOI: 10.1074/jbc.RA119.008133

Experimental method

X-RAY DIFFRACTION (2.1 Å)