Tail fiber function and structure | Bacteriophage T4 Tail
Bacteriophage T4 has two sets of tail fibers, long tail fibers that are the initial receptor binding proteins and short tail fibers that bind subsequently and trigger the
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Bacteriophage T4 has two sets of tail fibers, long tail fibers that are the initial receptor binding proteins and short tail fibers that bind subsequently and trigger the
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This regulation might prevent the inadvertent binding of the tail fibers to the host in conditions that are unfavorable. In vitro, retraction and extension can be controlled by pH, ionic strength, temperature
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Assembly of tail fibers from some bacteriophage requires the aid of an ''autochaperone'' as shown for the phi29 tail appendage . The precursor protein of the phi29 tail fiber contains an ATP
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Despite the wide occurrence of Tfa proteins, their functional mechanism has not been elucidated. Here, we investigate the tail fibre and Tfa of Escherichia coli phage Mu.
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Bacteriophages use receptor-binding proteins (RBPs) to adhere to bacterial hosts. Understanding the structure of these RBPs can provide insights into their target interactions. Tail
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The short tail fibre is hinged with the receptor-binding region hidden in the baseplate and enables binding, and it rotates and extends in a process
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Tail fibers are specialized protein appendages on bacteriophages that recognize and attach to specific bacterial host cell receptors, initiating viral infection.
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RBPseg enables accurate modeling of tail fiber structure, providing the first comprehensive tail fiber structure atlas.
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The tail fiber of phages contains receptor-binding proteins that bind with cell surface receptors . No presumed antibiotic resistance genes or virulence
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In this manuscript, we used a fusion protein comprised of an N-terminal bioluminescent tag translationally fused to T4''s long tail fiber binding tip (gp37) to evaluate and quantify gp37''s
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Organization of the bacteriophage T4 long tail fiber. (A) A structural model of bacteriophage T4 virion showing the head, the tail, and the long tail fibers.
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Here, we introduce RBPseg, a method that combines monomeric ESMFold predictions with a structural-based domain identification approach, to
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Bacteriophage lambda is an excellent model system to study the tail architecture of bacteriophages. Wang et al. present the cryo-EM structures of the components of the bacteriophage
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In this study, we identified a new structure of the podophage with three types of tail fibers, and such phages with different types of fibers may have a broad host range and/or infect host cells
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RBPseg workflow in detail, step-by-step demonstrating the 682 architecture of RBPseg using TC14 fiber as example. A FASTA file is input to ESMfold, which 683 generates a monomeric model.
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– and irreversibly bind to the outer core region of the lipopolysac-charides (12). This binding is followed by contraction of the outer tail sheath (13, 14), penetration of the bacterial membrane by the hollow
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The predicted structure of the tail fiber revealed that the two amino acid residues are located on the surface of the tail fiber, suggesting that these two
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In the case of phage T4, the initial recognition of the bacterial cell required for the infection, is carried out by the long tail fibers (depicted in Fig. 1a). These fibers reversibly bind to the outer glucose[α1
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At the first step of phage infection, the receptor-binding proteins (RBPs) such as tail fibers are responsible for recognizing specific host surface receptors. The proper folding and assembly of
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We fused C-terminal portions of J, the tail fiber protein of λ, to maltose-binding protein. Solid-phase binding assays demonstrated that a purified fusion protein
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To initiate their life cycle, phages must specifically bind to the surface of their bacterial hosts. Long-tailed phages often interact with the cell surface using fibers, which are elongated
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Here, we introduce RBPseg, a method that combines monomeric ESMFold predictions with a structural-based domain identification approach, to divide tail
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Phage host range is often determined by their long tail fibers (LTFs) that mediate adsorption of the virus particle to potential bacterial host cells, by binding to specific cell surface
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In this paper, we introduce RBPseg, a method that combines monomeric ESMfold predictions with a novel sigmoid distance pair (sDp) protein
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Tail fibers are long rod-shaped proteins positioned at the tip of the tail and bind specifically to proteins or carbohydrates exposed on the bacterial surface. They are diverse
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Here we utilized fluorescent reporter systems to characterize the effect of the side tail fibers on phage infection. We found that the side tail fibers interfere with phage DNA ejection
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Phage Proteins Required for Tail Fiber Assembly Also Bind Specifically to the Surface of Host Bacterial Strains.
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The Myoviridae-like tail-morphotype phages do not possess an MTP. Host cell recognition commences by the binding of the distal half-fibers of gp17 to the core heptose region of Escherichia
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This study shows that the tail tips, the most diversified region across bacteriophage lambda and other long-tailed phages (or tail-like machines),
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