Ontology highlight
ABSTRACT:
SUBMITTER: Halder S
PROVIDER: S-EPMC5740621 | biostudies-literature | 2017 Dec
REPOSITORIES: biostudies-literature
Halder Sabyasachi S Parrell Daniel D Whitten Douglas D Feig Michael M Kroos Lee L
Proceedings of the National Academy of Sciences of the United States of America 20171127 50
Intramembrane proteases (IPs) cleave membrane-associated substrates in nearly all organisms and regulate diverse processes. A better understanding of how these enzymes interact with their substrates is necessary for rational design of IP modulators. We show that interaction of <i>Bacillus subtilis</i> IP SpoIVFB with its substrate Pro-σ<sup>K</sup> depends on particular residues in the interdomain linker of SpoIVFB. The linker plus either the N-terminal membrane domain or the C-terminal cystathi ...[more]