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A "mechanistic" explanation of the multiple helical forms adopted by bacterial flagellar filaments.

Abstract：

:The corkscrew-like flagellar filaments emerging from the surface of bacteria such as Salmonella typhimurium propel the cells toward nutrient and away from repellents. This kind of motility depends upon the ability of the flagellar filaments to adopt a range of distinct helical forms. A filament is typically constructed from ~30,000 identical flagellin molecules, which self-assemble into a tubular structure containing 11 near-longitudinal protofilaments. A "mechanical" model, in which the flagellin building block has the capacity to switch between two principal interfacial states, predicts that the filament can assemble into a "canonical" family of 12 distinct helical forms, each having unique curvature and twist: these include two "extreme" straight forms having left- and right-handed twists, respectively, and 10 intermediate helical forms. Measured shapes of the filaments correspond well with predictions of the model. This report is concerned with two unanswered questions. First, what properties of the flagellin determine which of the 12 discrete forms is preferred? Second, how does the interfacial "switch" work, at a molecular level? Our proposed solution of these problems is based mainly on a detailed examination of differences between the available electron cryo-microscopy structures of the straight L and R filaments, respectively.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Calladine CR,Luisi BF,Pratap JV

doi

10.1016/j.jmb.2012.12.007

subject

Has Abstract

pub_date

2013-03-11 00:00:00

pages

914-28

issue

5

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(12)00940-0

journal_volume

425

pub_type

杂志文章

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