Photo by livvie_bruce from unsplash
The intramembrane rhomboid proteases are of particular interest due to their ability to hydrolyze a substrate peptide bond at the active site which is buried within the membrane. The high-resolution… Click to show full abstract
The intramembrane rhomboid proteases are of particular interest due to their ability to hydrolyze a substrate peptide bond at the active site which is buried within the membrane. The high-resolution structure of the E. coli rhomboid protease GlpG revealed the catalytic dyad Ser201/His254, which is surrounded by a protein matrix and connected to bulk water via a narrow water channel. Although multiple crystal structures have been solved for GlpG, its catalytic mechanism is not clearly understood.
Keywords:
rhomboid protease;
protease glpg;
bond;
active site
Journal Title: Biophysical Journal
Year Published: 2017
Link to full text (if available)
Share on Social Media: Sign Up to like & get
recommendations!
Journal Title: Biophysical Journal
Year Published: 2017
Link to full text (if available)
Share on Social Media: Sign Up to like & get
recommendations!