6F45

Crystal structure of the gp37-gp38 adhesin tip complex of the bacteriophage S16 long tail fiber

Summary for 6F45

• Entry DOI: 10.2210/pdb6f45/pdb
• Descriptor: Receptor recognition protein, Long tail fiber distal subunit, MAGNESIUM ION, ... (7 entities in total)
• Functional Keywords: bacteriophage, helical sandwich, tail fiber, polyglycine, viral protein
• Biological source: Salmonella phage vB_SenMS16; More
• Total number of polymer chains: 4
• Total formula weight: 94118.58

Authors

Dunne, M.,Leiman, P.,Klumpp, J.,Loessner, M.J. (deposition date: 2017-11-29, release date: 2018-08-01, Last modification date: 2024-05-08)

Primary citation

Dunne, M.,Denyes, J.M.,Arndt, H.,Loessner, M.J.,Leiman, P.G.,Klumpp, J.
Salmonella Phage S16 Tail Fiber Adhesin Features a Rare Polyglycine Rich Domain for Host Recognition.
Structure, 26:1573-1582.e4, 2018

PubMed Abstract: The ability of phages to infect specific bacteria has led to their exploitation as bio-tools for bacterial remediation and detection. Many phages recognize bacterial hosts via adhesin tips of their long tail fibers (LTFs). Adhesin sequence plasticity modulates receptor specificity, and thus primarily defines a phage's host range. Here we present the crystal structure of an adhesin (gp38) attached to a trimeric β-helical tip (gp37) from the Salmonella phage S16 LTF. Gp38 contains rare polyglycine type II helices folded into a packed lattice, herein designated "PG sandwich." Sequence variability within the domain is limited to surface-exposed helices and distal loops that form putative receptor-binding sites. In silico analyses revealed a prevalence of the adhesin architecture among T-even phages, excluding the archetypal T4 phage. Overall, S16 LTF provides a valuable model for understanding binding mechanisms of phage adhesins, and for engineering of phage adhesins with expandable or modulated host ranges.

PubMed: 30244968
DOI: 10.1016/j.str.2018.07.017

Experimental method

X-RAY DIFFRACTION (1.70355818561 Å)