6ZNI
Structure of the Shigella MxiH needle filament attached to the basal body
Summary for 6ZNI
Entry DOI | 10.2210/pdb6zni/pdb |
EMDB information | 11312 |
Descriptor | Protein MxiH (1 entity in total) |
Functional Keywords | type 3 secretion system, shigella, helical reconstruction, needle filament., protein transport |
Biological source | Shigella flexneri 5a str. M90T |
Total number of polymer chains | 23 |
Total formula weight | 254386.42 |
Authors | Lunelli, M.,Kotov, V.,Marlovits, T.C.,Kolbe, M. (deposition date: 2020-07-06, release date: 2021-07-07, Last modification date: 2024-05-01) |
Primary citation | Kotov, V.,Lunelli, M.,Wald, J.,Kolbe, M.,Marlovits, T.C. Helical reconstruction of Salmonella and Shigella needle filaments attached to type 3 basal bodies. Biochem Biophys Rep, 27:101039-101039, 2021 Cited by 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 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. PubMed: 34258394DOI: 10.1016/j.bbrep.2021.101039 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.6 Å) |
Structure validation
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