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| Title | Cryo-EM analysis of the SctV cytosolic domain from the enteropathogenic E. coli T3SS injectisome. |
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| Journal, issue, pages | J Struct Biol, Vol. 212, Issue 3, Page 107660, Year 2020 |
| Publish date | Dec 1, 2020 |
 Authors | Dorothy D Majewski / Bronwyn J E Lyons / Claire E Atkinson / Natalie C J Strynadka /  |
| PubMed Abstract | The bacterial injectisome and flagella both rely on type III secretion systems for their assembly. The syringe-like injectisome creates a continuous channel between the bacterium and the host cell, ...The bacterial injectisome and flagella both rely on type III secretion systems for their assembly. The syringe-like injectisome creates a continuous channel between the bacterium and the host cell, through which signal-modulating effector proteins are secreted. The inner membrane pore protein SctV controls the hierarchy of substrate selection and may also be involved in energizing secretion. We present the 4.7 Å cryo-EM structure of the SctV cytosolic domain (SctV) from the enteropathogenic Escherichia coli injectisome. SctV forms a nonameric ring with primarily electrostatic interactions between its subunits. Molecular dynamics simulations show that monomeric SctV maintains a closed conformation, in contrast with previous studies on flagellar homologue FlhA. Comparison with substrate-bound homologues suggest that a conformational change would be required to accommodate binding partners. |
 External links | J Struct Biol / PubMed:33129970 |
| Methods | EM (single particle) |
| Resolution | 4.6 - 4.7 Å |
| Structure data | EMDB-22589, PDB-7k08:  EMDB-22590: |
| Source |
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 Keywords | PROTEIN TRANSPORT / Injectisome / Nonamer / Export Apparatus / Secretion |
Escherichia coli O127:H6 str. E2348/69 (bacteria)