Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6ZNI

Structure of the Shigella MxiH needle filament attached to the basal body

Summary for 6ZNI
Entry DOI10.2210/pdb6zni/pdb
EMDB information11312
DescriptorProtein MxiH (1 entity in total)
Functional Keywordstype 3 secretion system, shigella, helical reconstruction, needle filament., protein transport
Biological sourceShigella flexneri 5a str. M90T
Total number of polymer chains23
Total formula weight254386.42
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 citationKotov, 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: 34258394
DOI: 10.1016/j.bbrep.2021.101039
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.6 Å)
Structure validation

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon