Dataset Information
CryoET of presequence protease single particle
Ontology highlight
ABSTRACT:
SUBMITTER: Wei-Jen Tang
PROVIDER: EMPIAR-10929 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Structural basis for the mechanisms of human presequence protease conformational switch and substrate recognition.
Nature communications 20220405 1
Presequence protease (PreP), a 117 kDa mitochondrial M16C metalloprotease vital for mitochondrial proteostasis, degrades presequence peptides cleaved off from nuclear-encoded proteins and other aggregation-prone peptides, such as amyloid β (Aβ). PreP structures have only been determined in a closed conformation; thus, the mechanisms of substrate binding and selectivity remain elusive. Here, we leverage advanced vitrification techniques to overcome the preferential denaturation of one of two ~55 ...[more]