HOME / Catalysis of bundled tail fibers - Umele Photonics & Micro-Optics Europe
Here, we introduce RBPseg, a method that combines monomeric ESMFold predictions with a structural- based domain identi cation approach, to divide tail ber sequences into manageable fractions for high-
Bacteriophage T4 initially recognizes its host cells using its long tail fibers. Long tail fibers consist of a phage-proximal and a phage-distal rod, each around 80 nm long and attached to each
The exact mechanisms of how the tail fiber interacts with the receptor at the molecular/atomic level are critical for engineering phages with reprogrammed host ranges. The advancement of technologies
Using this approach, we generated complete tail fiber models, validated by single- particle cryo–electron microscopy of five fibers from three phages. A structural classification of 67 fibers
Download Citation | Phage Proteins Required for Tail Fiber Assembly Also Bind Specifically to the Surface of Host Bacterial Strains | With the growing interest in using phages to
18 Tail fibers, a prominent type of RBP, are typically elongated, flexible, and trimeric proteins, 19 making it challenging to obtain high-resolution experimental data of their full-length structures. 20 Recent
Bacterial transduction particles were critical to early advances in molecular biology and are currently experiencing a resurgence in interest within the diagnostic and therapeutic fields. The
Providing detailed structures of bacteriophage lambda infection initiation, this study contributes to the expanding knowledge of lambda-bacterial interaction, which holds significance in
Bacteriophage libraries containing millions of variants of phage tail fiber motifs on a common structural scaffold give rise to infectious phages with expanded or altered host ranges, which may be useful for
It is shown that adsorbability of T4 is regularly correlated with the extended state of the tail fibers, suggesting that in T4 fiber extension is a necessary condition for adsorption. Abstract It is shown that
In this study, we analyzed the tail fibers of published Acinetobacter phages and identified different functional domains present. These data will enable further research and development on
Structural analysis enabled us to propose the assembly mechanism of phage tail fibers, in which the chaperone first protects the intertwined and repetitive distal moiety of each fiber subunit,
This study addresses these gaps by offering an in-depth review of the entire lifecycle of cattail fibers, from species identification and fiber extraction techniques to
We identified 3,445 eCIS tail fiber proteins found in 2,585 eCIS loci from 1,069 microbes. These fibers can be categorized by five new N-terminal domains responsible for tail fiber attachment to eCIS
Download scientific diagram | Protein domains identified in A. baumannii tail fibers analyzed with InterProScan: pectin lyase-like domain (PLD; blue), tailspike binding protein (TSB; orange
The crystal structure of a complex between the tail fibre and tail fibre assembly (Tfa) protein of Escherichia coli phage Mu reveals the mechanisms by which Tfa regulates fibre assembly
While this manuscript only demonstrates our assay''s ability to characterize adsorptive capabilities of phage tail fibers, our assay could feasibly be modified to evaluate other adsorption
Tail fiber proteins derived from the tail fibers of bacteriophages can recognize specific bacterial surface polysaccharides. For example, recombinant tail proteins, such as TF2 and TF6
Bacteriophage lambda has a double-stranded DNA genome and a long, flexible, non-contractile tail encoded by a contiguous block of 11 genes downstream of the head genes. The tail
In this study, we determined the X-ray structure of the C -terminal LPS-binding domain of the Mu (−) tail fiber, the alternative tail fiber gp52, to understand the mechanism by which the two tail
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
These hollow elongated protein structures, present in most bacteriophages of the order Caudovirales, connect the DNA-containing capsid with a receptor function at the distal end of the tail