7K08
Cryo-EM structure of the nonameric EscV cytosolic domain from the type III secretion system
Summary for 7K08
| Entry DOI | 10.2210/pdb7k08/pdb |
| EMDB information | 22589 22590 |
| Descriptor | Translocator EscV (1 entity in total) |
| Functional Keywords | injectisome, nonamer, export apparatus, secretion, protein transport |
| Biological source | Escherichia coli O127:H6 (strain E2348/69 / EPEC) |
| Total number of polymer chains | 9 |
| Total formula weight | 351734.70 |
| Authors | Majewski, D.D.,Lyons, B.J.E.,Atkinson, C.E.,Strynadka, N.C.J. (deposition date: 2020-09-03, release date: 2020-11-25, Last modification date: 2024-03-06) |
| Primary citation | Majewski, D.D.,Lyons, B.J.E.,Atkinson, C.E.,Strynadka, N.C.J. Cryo-EM analysis of the SctV cytosolic domain from the enteropathogenic E. coli T3SS injectisome. J.Struct.Biol., 212:107660-107660, 2020 Cited by 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, 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. PubMed: 33129970DOI: 10.1016/j.jsb.2020.107660 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.7 Å) |
Structure validation
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