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000912262 0247_ $$2doi$$a10.1016/j.jbc.2021.101472
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000912262 0247_ $$2ISSN$$a1083-351X
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000912262 1001_ $$0P:(DE-HGF)0$$aZinke, Maximilian$$b0$$eCorresponding author
000912262 245__ $$aMajor tail proteins of bacteriophages of the order Caudovirales
000912262 260__ $$aBethesda, Md.$$bSoc.$$c2022
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000912262 520__ $$aTechnological advances in cryo-EM in recent years have given rise to detailed atomic structures of bacteriophage tail tubes—a class of filamentous protein assemblies that could previously only be studied on the atomic scale in either their monomeric form or when packed within a crystal lattice. These hollow elongated protein structures, present in most bacteriophages of the order Caudovirales, connect the DNA-containing capsid with a receptor function at the distal end of the tail and consist of helical and polymerized major tail proteins. However, the resolution of cryo-EM data for these systems differs enormously between different tail tube types, partly inhibiting the building of high-fidelity models and barring a combination with further structural biology methods. Here, we review the structural biology efforts within this field and highlight the role of integrative structural biology approaches that have proved successful for some of these systems. Finally, we summarize the structural elements of major tail proteins and conceptualize how different amounts of tail tube flexibility confer heterogeneity within cryo-EM maps and, thus, limit high-resolution reconstructions.
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000912262 7001_ $$0P:(DE-Juel1)132018$$aSchröder, Gunnar F.$$b1$$ufzj
000912262 7001_ $$00000-0002-7534-5973$$aLange, Adam$$b2$$eCorresponding author
000912262 773__ $$0PERI:(DE-600)1474604-9$$a10.1016/j.jbc.2021.101472$$gVol. 298, no. 1, p. 101472 -$$n1$$p101472 -$$tThe journal of biological chemistry$$v298$$x0021-9258$$y2022
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000912262 9141_ $$y2022
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