Ontology highlight
ABSTRACT:
SUBMITTER: Zoll S
PROVIDER: S-EPMC4253528 | biostudies-literature | 2014 Oct
REPOSITORIES: biostudies-literature
Zoll Sebastian S Stanchev Stancho S Began Jakub J Skerle Jan J Lepšík Martin M Peclinovská Lucie L Majer Pavel P Strisovsky Kvido K
The EMBO journal 20140912 20
The mechanisms of intramembrane proteases are incompletely understood due to the lack of structural data on substrate complexes. To gain insight into substrate binding by rhomboid proteases, we have synthesised a series of novel peptidyl-chloromethylketone (CMK) inhibitors and analysed their interactions with Escherichia coli rhomboid GlpG enzymologically and structurally. We show that peptidyl-CMKs derived from the natural rhomboid substrate TatA from bacterium Providencia stuartii bind GlpG in ...[more]