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Cryo-EM structure of the bacteria-killing type IV secretion system core complex from Xanthomonas citri
- Source :
- Nature microbiology
- Publication Year :
- 2018
- Publisher :
- Nature Publishing Group, 2018.
-
Abstract
- Type IV secretion (T4S) systems form the most common and versatile class of secretion systems in bacteria, capable of injecting both proteins and DNAs into host cells. T4S systems are typically composed of 12 components that form 2 major assemblies: the inner membrane complex embedded in the inner membrane and the core complex embedded in both the inner and outer membranes. Here we present the 3.3 A-resolution cryo-electron microscopy model of the T4S system core complex from Xanthomonas citri, a phytopathogen that utilizes this system to kill bacterial competitors. An extensive mutational investigation was performed to probe the vast network of protein–protein interactions in this 1.13-MDa assembly. This structure expands our knowledge of the molecular details of T4S system organization, assembly and evolution. A combination of cryo-electron microscopy (cryo-EM) and targeted mutagenesis studies elucidates the structure and organization of the core complex of the type IV secretion system used by Xanthomonas citri to kill competing bacteria.
- Subjects :
- Microbiology (medical)
Models, Molecular
Protein Conformation, alpha-Helical
Xanthomonas
Cryo-electron microscopy
PROTEINS
Protein Conformation
Immunology
Mutagenesis (molecular biology technique)
BIOLOGY
bcs
Applied Microbiology and Biotechnology
Microbiology
Article
Xanthomonas citri
Type IV Secretion Systems
03 medical and health sciences
Bacterial Proteins
1108 Medical Microbiology
Genetics
Inner membrane
Secretion
Protein Interaction Domains and Motifs
Cloning, Molecular
030304 developmental biology
0303 health sciences
Inner membrane complex
Science & Technology
biology
Bacteria
030306 microbiology
Chemistry
Cryoelectron Microscopy
Cell Biology
Gene Expression Regulation, Bacterial
biology.organism_classification
Membrane protein
Multiprotein Complexes
Mutation
Biophysics
VISUALIZATION
Life Sciences & Biomedicine
Bacterial Outer Membrane Proteins
Protein Binding
0605 Microbiology
Subjects
Details
- Language :
- English
- ISSN :
- 20585276
- Database :
- OpenAIRE
- Journal :
- Nature microbiology
- Accession number :
- edsair.doi.dedup.....86a38977066a6b6f449a0d075aa78ce9