Phage Proteins Required for Tail Fiber Assembly Also Bind
Tail fiber assembly (Tfa) proteins are a very large family of proteins that serve as chaperones for fiber folding in a wide variety of phages that infect diverse species.
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Fiber Tail Folding Range
Targeting mechanisms of tailed bacteriophages
This innovative paper describes how the host range of R-type pyocins can be reprogrammed by replacing parts of the tail fibres between phages with different host ranges.
Towards a complete phage tail fiber structure atlas
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.
Chromatin Fiber Folding Directed by Cooperative Histone Tail
To explore the folding propensity by which these features may govern gene expression, we analyze 20 kb fibers that contain regularly spaced acetylation islands of two sizes (2 or 5 kb) with
Understanding Bacteriophage Tail Fiber Interaction with Host
In this review, we comprehensively summarize how the tail fibers of the T4 phage recognize host surface receptors at single-molecule and atomic levels.
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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
RBPseg: Toward a complete phage tail fiber structure atlas
Here, we introduce RBPseg, a method that combines monomeric ESMFold predictions with a structural-based domain identification approach, to divide tail fiber sequences into manageable
Structural Insights into the Chaperone-Assisted Assembly of a
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 tail
Engineering Phage Host-Range and Suppressing Bacterial
Through natural evolution and structural modeling, we identified host-range-determining regions (HRDRs) in the T3 phage tail fiber protein and developed a high-throughput strategy to genetically
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RBPs play a critical role in spatial and temporal positioning of the tail apparatus to the bacterial surface during infection. High-resolution structures of RBPs can be used as ''blueprints'' to
Phage tail fibre assembly proteins employ a modular structure to drive
We find that Tfa proteins are comprised of two domains: a non-conserved N-terminal domain that binds to the C-terminal region of the fibre and a conserved C-terminal domain that