Structural flexibility of the tetanus neurotoxin revealed by crystallographic and solution scattering analyses.

ABSTRACT: Although the tetanus neurotoxin (TeNT) delivers its protease domain (LC) across the synaptic vesicle lumen into the cytosol via its receptor binding domain (H_C) and translocation domain (H_N), the molecular mechanism coordinating this membrane translocation remains unresolved. Here, we report the high-resolution crystal structures of full-length reduced TeNT (rTeNT, 2.3 Å), TeNT isolated H_N (TeNT/iH_N, 2.3 Å), TeNT isolated H_C (TeNT/iH_C, 1.5 Å), together with the solution structures of TeNT/iH_N and beltless TeNT/iH_N (TeNT/blH_N). TeNT undergoes significant domains rotation of the H_N and LC were demonstrated by structural comparison of rTeNT and non-reduced-TeNT (nrTeNT). A linker loop

SUBMITTER: Zhang CM 

PROVIDER: S-EPMC7868712 | biostudies-literature | 2021

REPOSITORIES: biostudies-literature