4QNL
Crystal structure of tail fiber protein gp63.1 from E. coli phage G7C
Summary for 4QNL
| Entry DOI | 10.2210/pdb4qnl/pdb |
| Descriptor | Tail fiber protein, DI(HYDROXYETHYL)ETHER, 1,2-ETHANEDIOL, ... (7 entities in total) |
| Functional Keywords | tail fiber; g7c phage; hydrolase-type esterase;, sgnh hydrolase-type esterase domain (ipr013831), adsorption of the phage on bacterial host, bacterial lps digestion, tail fiber protein gp66, selenomethionine derivative, distal end of the baseplate, hydrolase |
| Biological source | Escherichia phage vB_EcoP_G7C |
| Total number of polymer chains | 1 |
| Total formula weight | 95584.31 |
| Authors | Riccio, C.,Browning, C.,Prokhorov, N.,Letarov, A.,Leiman, P.G. (deposition date: 2014-06-18, release date: 2015-06-24, Last modification date: 2024-10-09) |
| Primary citation | Prokhorov, N.S.,Riccio, C.,Zdorovenko, E.L.,Shneider, M.M.,Browning, C.,Knirel, Y.A.,Leiman, P.G.,Letarov, A.V. Function of bacteriophage G7C esterase tailspike in host cell adsorption. Mol. Microbiol., 105:385-398, 2017 Cited by PubMed Abstract: Bacteriophages recognize and bind to their hosts with the help of receptor-binding proteins (RBPs) that emanate from the phage particle in the form of fibers or tailspikes. RBPs show a great variability in their shapes, sizes, and location on the particle. Some RBPs are known to depolymerize surface polysaccharides of the host while others show no enzymatic activity. Here we report that both RBPs of podovirus G7C - tailspikes gp63.1 and gp66 - are essential for infection of its natural host bacterium E. coli 4s that populates the equine intestinal tract. We characterize the structure and function of gp63.1 and show that unlike any previously described RPB, gp63.1 deacetylates surface polysaccharides of E. coli 4s leaving the backbone of the polysaccharide intact. We demonstrate that gp63.1 and gp66 form a stable complex, in which the N-terminal part of gp66 serves as an attachment site for gp63.1 and anchors the gp63.1-gp66 complex to the G7C tail. The esterase domain of gp63.1 as well as domains mediating the gp63.1-gp66 interaction is widespread among all three families of tailed bacteriophages. PubMed: 28513100DOI: 10.1111/mmi.13710 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.411 Å) |
Structure validation
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