Article
In vivo analysis reveals substrate-gating mutants of a rhomboid intramembrane protease display increased activity in living cells.
Biological chemistry - 1 Aug 2008
Urban Sinisa, Baker Rosanna P
Abstract excerpt
Intramembrane proteases hydrolyze peptide bonds within cell membranes. Recent crystal structures revealed that rhomboid intramembrane proteases contain a hydrated active site that opens to the outside of the cell, but is protected laterally from membrane lipids by protein segments. Using Escherichia coli rhomboid (GlpG) structures as a guide, we previously took a mutational approach to identify the GlpG gating...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.
