7A27
Structure of soluble SmhA crystal form 2 of the tripartite alpha-pore forming toxin, Smh, from Serratia marcescens.
This is a non-PDB format compatible entry.
Summary for 7A27
| Entry DOI | 10.2210/pdb7a27/pdb |
| Descriptor | SmhA (2 entities in total) |
| Functional Keywords | pore forming toxin, toxin, bacterial toxin, serratia marcescens |
| Biological source | Serratia marcescens |
| Total number of polymer chains | 4 |
| Total formula weight | 159905.11 |
| Authors | Churchill-Angus, A.M.,Baker, P.J. (deposition date: 2020-08-16, release date: 2021-03-31, Last modification date: 2024-01-31) |
| Primary citation | Churchill-Angus, A.M.,Schofield, T.H.B.,Marlow, T.R.,Sedelnikova, S.E.,Wilson, J.S.,Rafferty, J.B.,Baker, P.J. Characterisation of a tripartite alpha-pore forming toxin from Serratia marcescens Sci Rep, 11:6447-, 2021 Cited by PubMed Abstract: Tripartite members of the ClyA family of α-PFTs have recently been identified in a number of pathogenic Gram-negative bacteria, including the human pathogen Serratia marcescens. Structures of a Gram-negative A component and a tripartite α-PFT complete pore are unknown and a mechanism for pore formation is still uncertain. Here we characterise the tripartite SmhABC toxin from S. marcescens and propose a mechanism of pore assembly. We present the structure of soluble SmhA, as well as the soluble and pore forms of SmhB. We show that the β-tongue soluble structure is well conserved in the family and propose two conserved latches between the head and tail domains that are broken on the soluble to pore conformational change. Using the structures of individual components, sequence analysis and docking predictions we illustrate how the A, B and C protomers would assemble on the membrane to produce a complete tripartite α-PFT pore. PubMed: 33742033DOI: 10.1038/s41598-021-85726-0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.57 Å) |
Structure validation
Download full validation report
