Rhomboid Protease

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I. Introduction

Rhomboid proteases are a family of proteins that cleave the transmembrane domain of membrane proteins.  An example of a rhomboid protein is GlpG, found in the membrane of Escherichia coli.  GlpG and all other rhomboid proteases have six hydrophobic segments that span the membrane and give the enzyme a serpentine characteristic.

For more information see Biochemistry Online: Chapter 7B - Mechanisms of Enzyme Catalysis

II. General Structure

Backbone and sidechains with highlighted transmembrane subunits
Rhomboid with transmembrane helices represented as barrels or "Rockets"
Protein backbone with highlighted subunits and prominent residues (colored pink) in the active site

Protein backbone with prominent residues in the active site in the presence of water

L1 subunit (colored gray) and prominent residues (colored yellow) in the active site in the presence of water (colored red).
Protein (spacefill) interacting with DNA
Protein backbone and Hbonds in the presence of water