AbstractThis report describes the structure of a putative tail fiber protein of the Acinetobacter baumannii bacteriophage AP22. The target host range of strictly lytic bacteriophage AP22 includes many clinical isolates of A. baumannii from hospitals in Chelyabinsk, Nizhny Novgorod, Moscow and St. Petersburg (Russia), but its host cell binding apparatus remains uncharacterized. Here, we report the crystal structure of the C-terminal fragment of AP22 gene product 53 (gp53) one of its two putative host cell-binding proteins. We show that gp53 forms a trimeric fiber and binds ethylene glycol and glycerol molecules that represent known surrogates of the oligosaccharide backbone. However, despite its structural similarities to other phage/virus host cell-binding fibers and its binding to small sugar-like molecules, gp53 did not inhibit AP22 infection and its role in the infection process remains unclear.
Crystal Structure of the Carboxy-Terminal Region of the Bacteriophage T4 Proximal Long Tail Fiber Protein Gp34