Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structural basis for host recognition and superinfection exclusion by bacteriophage T5.
Journal, issue, pages	Proc Natl Acad Sci U S A, Vol. 119, Issue 42, Page e2211672119, Year 2022
Publish date	Oct 18, 2022
Authors	Bert van den Berg / Augustinas Silale / Arnaud Baslé / Astrid F Brandner / Sophie L Mader / Syma Khalid /
PubMed Abstract	A key but poorly understood stage of the bacteriophage life cycle is the binding of phage receptor-binding proteins (RBPs) to receptors on the host cell surface, leading to injection of the phage ...A key but poorly understood stage of the bacteriophage life cycle is the binding of phage receptor-binding proteins (RBPs) to receptors on the host cell surface, leading to injection of the phage genome and, for lytic phages, host cell lysis. To prevent secondary infection by the same or a closely related phage and nonproductive phage adsorption to lysed cell fragments, superinfection exclusion (SE) proteins can prevent the binding of RBPs via modulation of the host receptor structure in ways that are also unclear. Here, we present the cryogenic electron microscopy (cryo-EM) structure of the phage T5 outer membrane (OM) receptor FhuA in complex with the T5 RBP pb5, and the crystal structure of FhuA complexed to the OM SE lipoprotein Llp. Pb5 inserts four loops deeply into the extracellular lumen of FhuA and contacts the plug but does not cause any conformational changes in the receptor, supporting the view that DNA translocation does not occur through the lumen of OM channels. The FhuA-Llp structure reveals that Llp is periplasmic and binds to a nonnative conformation of the plug of FhuA, causing the inward folding of two extracellular loops via "reverse" allostery. The inward-folded loops of FhuA overlap with the pb5 binding site, explaining how Llp binding to FhuA abolishes further infection of by phage T5 and suggesting a mechanism for SE via the jamming of TonB-dependent transporters by small phage lipoproteins.
External links	Proc Natl Acad Sci U S A / PubMed:36215462 / PubMed Central
Methods	EM (single particle) / X-ray diffraction
Resolution	3.1 - 3.37 Å
Structure data	15229 8a8c EMDB-15229, PDB-8a8c: T5 phage receptor-binding protein pb5 bound to ferrichrome transporter FhuA Method: EM (single particle) / Resolution: 3.1 Å PDB-8a60: Crystal structure of FhuA in complex with the superinfection exclusion lipoprotein Llp Method: X-RAY DIFFRACTION / Resolution: 3.37 Å
Chemicals	ChemComp-LU9: [(2R,3S,4R,5R,6R)-2-[[(2R,4R,5R,6R)-6-[(1R)-1,2-bis(oxidanyl)ethyl]-4-[(2R,4R,5R,6R)-6-[(1R)-1,2-bis(oxidanyl)ethyl]-2-carboxy-4,5-bis(oxidanyl)oxan-2-yl]oxy-2-carboxy-5-oxidanyl-oxan-2-yl]oxymethyl]-5-[[(3R)-3-dodecanoyloxytetradecanoyl]amino]-4-(3-nonanoyloxypropanoyloxy)-6-[[(2R,3S,4R,5R,6R)-3-oxidanyl-4-[(3S)-3-oxidanyltetradecanoyl]oxy-5-[[(3R)-3-oxidanyltridecanoyl]amino]-6-phosphonatooxy-oxan-2-yl]methoxy]oxan-3-yl] phosphate / toxin*YM / Lipopolysaccharide
Source	escherichia phage t5 (virus) escherichia coli k-12 (bacteria)
Keywords	MEMBRANE PROTEIN / Outer membrane TonB-dependent transporter FhuA Bacteriophage T5 Superinfection exclusion E. coli / Bacteriophage / receptor / TonB-dependent transporter / outer membrane