6f45 | pdb_00006f45

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

spinqualitylabelsall models 6f45, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6f45 is a 4 chain structure with sequence from Salmonella phage vB_SenM-S16. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.7035582Å Ligands: IMD, MG, MPD, MRD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function M1EBB2_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 PubMed 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 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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