6f45
From Proteopedia
Crystal structure of the gp37-gp38 adhesin tip complex of the bacteriophage S16 long tail fiber
Structural highlights
FunctionM1EBB2_BPS16 Vg38 is at the tip of the long tail fibers and serves as the phage recognition site for the cellular receptor.[ARBA:ARBA00003549] Publication Abstract from PubMedThe 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 beta-helical tip (gp37) from the Salmonella phage S16 LTF. Gp38 contains rare polyglycine type II helices folded into a packed lattice, herein designated "PGII 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. Salmonella Phage S16 Tail Fiber Adhesin Features a Rare Polyglycine Rich Domain for Host Recognition.,Dunne M, Denyes JM, Arndt H, Loessner MJ, Leiman PG, Klumpp J Structure. 2018 Aug 16. pii: S0969-2126(18)30263-6. doi:, 10.1016/j.str.2018.07.017. PMID:30244968[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||||
