ArticleActa crystallographica. Section F, Structural biology and crystallization communications2007
Expression, purification and preliminary crystallographic characterization of FlhF from Bacillus subtilis.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- FlhF interacts with TonB2 to defend against oxidative stress in Campylobacter jejuni.BMC microbiology · 2026Article
- Where and how many: evolutionary diversification of a molecular switch regulating flagellar patterns.Journal of bacteriology · 2026Review
- Role of FlhF and its domains in the assembly of a polar flagellum inJournal of bacteriology · 2025Article
- Structure of the GDP-bound state of the SRP GTPase FlhF.Acta crystallographica. Section F, Structural biology communications · 2024Article
- FlhF regulates the number and configuration of periplasmic flagella in Borrelia burgdorferi.Molecular microbiology · 2020Article
- The GTPase activity of FlhF is dispensable for flagellar localization, but not motility, in Pseudomonas aeruginosa.Journal of bacteriology · 2013Article
- The crystal structure of the third signal-recognition particle GTPase FlhF reveals a homodimer with bound GTP.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The gram-positive bacterium Bacillus subtilis contains three proteins belonging to the signal recognition particle (SRP) type GTPase family. The well characterized signal sequence-binding protein SRP54 and the SRP receptor protein FtsY are universally conserved components of the SRP system of protein transport. The third member, FlhF, has been implicated in the placement and assembly of polar flagella. This article describes the overexpression and preliminary X-ray crystallographic analysis of an FlhF fragment that corresponds to the well characterized GTPase domains in SRP54 and FtsY. Three crystal forms are reported with either GDP or GMPPNP and diffract to a resolution of about 3 A.
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