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Crystal structure and self-interaction of the type VI secretion tail-tube protein from enteroaggregative Escherichia coli
- Source :
- PLoS ONE, PLoS ONE, Public Library of Science, 2014, 9 (2), pp.e86918. ⟨10.1371/journal.pone.0086918⟩, PLoS ONE, 2014, 9 (2), pp.e86918. ⟨10.1371/journal.pone.0086918⟩, 'PloS One ', vol: 9, pages: e86918-1-e86918-9 (2014), PLoS ONE, Vol 9, Iss 2, p e86918 (2014)
- Publication Year :
- 2014
- Publisher :
- HAL CCSD, 2014.
-
Abstract
- International audience; The type VI secretion system (T6SS) is a widespread machine used by bacteria to control their environment and kill or disable bacterial species or eukaryotes through toxin injection. The T6SS comprises a central tube formed of stacked hexamers of hemolysin co-regulated proteins (Hcp) and terminated by a trimeric valine-glycine repeat protein G (VgrG) component, the cell puncturing device. A contractile tail sheath, formed by the TssB and TssC proteins, surrounds this tube. This syringe-like machine has been compared to an inverted phage, as both Hcp and VgrG share structural homology with tail components of Caudovirales. Here we solved the crystal structure of a tryptophan-substituted double mutant of Hcp1 from enteroaggregative Escherichia coli and compared it to the structures of other Hcps. Interestingly, we observed that the purified Hcp native protein is unable to form tubes in vitro. To better understand the rationale for observation, we measured the affinity of Hcp1 hexamers with themselves by surface plasmon resonance. The intra-hexamer interaction is weak, with a K D value of 7.2 mM. However, by engineering double cysteine mutants at defined positions, tubes of Hcp1 gathering up to 15 stacked hexamers formed in oxidative conditions. These results, together with those available in the literature regarding TssB and TssC, suggest that assembly of the T6SS tube differs significantly from that of Sipho-or Myoviridae.
- Subjects :
- Macromolecular Assemblies
Models, Molecular
Mutant Proteins/chemistry/metabolism
Light
[SDV]Life Sciences [q-bio]
lcsh:Medicine
Plasma protein binding
medicine.disease_cause
[SDV.BBM.BM] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology
Crystallography, X-Ray
Biochemistry
Transmembrane Transport Proteins
Protein structure
Escherichia coli/*metabolism
Escherichia coli Proteins/*chemistry/*metabolism/ultrastructure
Scattering, Radiation
Bacteriophages
Disulfides
lcsh:Science
Bacterial Secretion Systems
Peptide sequence
[SDV.BBM.BC] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM]
ComputingMilieux_MISCELLANEOUS
0303 health sciences
Multidisciplinary
biology
[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM]
Chemistry
Escherichia coli Proteins
030302 biochemistry & molecular biology
Recombinant Proteins
Bacterial Biochemistry
[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM]
[SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biophysics
[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM]
Disulfides/metabolism
Pseudomonas aeruginosa
Chromatography, Gel
Research Article
Protein Binding
Plasmons
Virulence Factors
[SDV.BBM.BS] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM]
Molecular Sequence Data
Biophysics
[SDV.BBM.BP] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biophysics
Myoviridae
Microbiology
Crystals
03 medical and health sciences
Secretion systems
Caudovirales
Escherichia coli
medicine
Protein structure comparison
[SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology
Amino Acid Sequence
[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM]
Protein Interactions
Biology
030304 developmental biology
Type VI secretion system
Crystal structure
lcsh:R
Proteins
Bacteriology
[SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology
Surface Plasmon Resonance
biology.organism_classification
Virulence Factors/*chemistry/*metabolism
Structural Homology, Protein
biology.protein
lcsh:Q
Mutant Proteins
Protein G
Protein Multimerization
Sequence Alignment
Subjects
Details
- Language :
- English
- ISSN :
- 19326203
- Database :
- OpenAIRE
- Journal :
- PLoS ONE, PLoS ONE, Public Library of Science, 2014, 9 (2), pp.e86918. ⟨10.1371/journal.pone.0086918⟩, PLoS ONE, 2014, 9 (2), pp.e86918. ⟨10.1371/journal.pone.0086918⟩, 'PloS One ', vol: 9, pages: e86918-1-e86918-9 (2014), PLoS ONE, Vol 9, Iss 2, p e86918 (2014)
- Accession number :
- edsair.doi.dedup.....61ff8f216af54e49d62e9d04ecd99a06