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-Structure paper
Title | Helical reconstruction of and needle filaments attached to type 3 basal bodies. |
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Journal, issue, pages | Biochem Biophys Rep, Vol. 27, Page 101039, Year 2021 |
Publish date | Jun 27, 2021 |
Authors | Vadim Kotov / Michele Lunelli / Jiri Wald / Michael Kolbe / Thomas C Marlovits / |
PubMed Abstract | Gram-negative pathogens evolved a syringe-like nanomachine, termed type 3 secretion system, to deliver protein effectors into the cytoplasm of host cells. An essential component of this system is a ...Gram-negative pathogens evolved a syringe-like nanomachine, termed type 3 secretion system, to deliver protein effectors into the cytoplasm of host cells. An essential component of this system is a long helical needle filament that protrudes from the bacterial surface and connects the cytoplasms of the bacterium and the eukaryotic cell. Previous structural research was predominantly focused on reconstituted type 3 needle filaments, which lacked the biological context. In this work we introduce a facile procedure to obtain high-resolution cryo-EM structure of needle filaments attached to the basal body of type 3 secretion systems. We validate our approach by solving the structure of PrgI filament and demonstrate its utility by obtaining the first high-resolution cryo-EM reconstruction of Shigella MxiH filament. Our work paves the way to systematic structural characterization of attached type 3 needle filaments in the context of mutagenesis studies, protein structural evolution and drug development. |
External links | Biochem Biophys Rep / PubMed:34258394 / PubMed Central |
Methods | EM (helical sym.) |
Resolution | 3.6 Å |
Structure data | EMDB-11311, PDB-6znh: EMDB-11312, PDB-6zni: |
Source |
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Keywords | PROTEIN TRANSPORT / Type 3 secretion system / Salmonella / Helical reconstruction / Needle filament. / Shigella |