作者:
Bloch, MagnusRaj, IshaPape, Tillmann HannsTaylor, Nicholas M.I.Structural Biology of Molecular Machines Group
Protein Structure & Function Program Novo Nordisk Foundation Center for Protein Research Faculty of Health and Medical Sciences University of Copenhagen Blegdamsvej 3B Copenhagen2200 Denmark Structural Molecular Biology Group
Protein Structure & Function Program Novo Nordisk Foundation Centre for Protein Research Faculty of Health and Medical Sciences University of Copenhagen Blegdamsvej 3B Copenhagen2200 Denmark
Faculty of Health and Medical Sciences University of Copenhagen Nørre Allé 20 Copenhagen2200 Denmark
Multidrug resistance-associated protein 4 (MRP4) is an ATP-binding cassette (ABC) transporter expressed at multiple tissue barriers where it actively extrudes a wide variety of drug compounds. Overexpression of MRP4 p...
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Bacteriophages in the Agtrevirus genus are known for expressing multiple tail spike proteins (TSPs), but little is known about their genetic diversity and host recognition apart from their ability to infect diverse En...
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Bacteriophages use receptor-binding proteins (RBPs) to adhere to bacterial hosts, yet their sequence and structural diversity remain poorly understood. Tail fibers, a major class of RBPs, are elongated and flexible tr...
Bacteriophages use receptor-binding proteins (RBPs) to adhere to bacterial hosts, yet their sequence and structural diversity remain poorly understood. Tail fibers, a major class of RBPs, are elongated and flexible trimeric proteins, making their full-length structures difficult to resolve experimentally. Advances in deep learning-based protein structure prediction, such as AlphaFold2-multimer (AF2M) and ESMFold, provide opportunities for studying these challenging proteins. 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 fractions for high-confidence modeling with AF2M. 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 identified 16 distinct classes and 89 domains, revealing patterns of modularity, convergence, divergence, and domain swapping. Our findings suggest that these structural classes represent at least 24% of the known tail fiber universe, providing key insights into their evolution and functionality.
Many bacteria use the flagellum for locomotion and chemotaxis. Its bidirectional rotation is driven by the membrane-embedded motor, which uses energy from the transmembrane ion gradient to generate torque at the inter...
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The arms race between bacteria and phages led to the evolution of a wide range of anti-phage defences, several of which are controlled by host cell quorum sensing. In this work we characterize a novel quorum sensing a...
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Many pairwise additive force fields are in active use for intrinsically disordered proteins (IDPs) and regions (IDRs), some of which modify energetic terms to improve description of IDPs/IDRs, but are largely in disag...
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Characterization of proteins with intrinsic or unfolded state disorder comprises a new frontier in structural biology, requiring the characterization of diverse and dynamic structural ensembles. We introduce a compreh...
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In the PDF version of this Article, owing to a typesetting error, an incorrect figure was used for Extended Data Fig. 5; the correct figure was used in the HTML version. This has been corrected online.
In the PDF version of this Article, owing to a typesetting error, an incorrect figure was used for Extended Data Fig. 5; the correct figure was used in the HTML version. This has been corrected online.
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