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Crystal structure of a rhomboid family intramembrane protease
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Crystal structure of a rhomboid family intramembrane protease
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Crystal structure of a rhomboid family intramembrane protease
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Journal Article
Crystal structure of a rhomboid family intramembrane protease
2006
Overview
Escherichia coli GlpG is an integral membrane protein that belongs to the widespread rhomboid protease family. Rhomboid proteases, like site-2 protease (S2P) and gamma-secretase, are unique in that they cleave the transmembrane domain of other membrane proteins. Here we describe the 2.1 A resolution crystal structure of the GlpG core domain. This structure contains six transmembrane segments. Residues previously shown to be involved in catalysis, including a Ser-His dyad, and several water molecules are found at the protein interior at a depth below the membrane surface. This putative active site is accessible by substrate through a large 'V-shaped' opening that faces laterally towards the lipid, but is blocked by a half-submerged loop structure. These observations indicate that, in intramembrane proteolysis, the scission of peptide bonds takes place within the hydrophobic environment of the membrane bilayer. The crystal structure also suggests a gating mechanism for GlpG that controls substrate access to its hydrophilic active site.
Publisher
Nature Publishing,Nature Publishing Group
Subject
/ Biological and medical sciences
/ DNA-Binding Proteins - chemistry
/ DNA-Binding Proteins - classification
/ DNA-Binding Proteins - metabolism
/ E coli
/ Endopeptidases - classification
/ Escherichia coli - enzymology
/ Escherichia coli Proteins - chemistry
/ Escherichia coli Proteins - classification
/ Escherichia coli Proteins - metabolism
/ Fundamental and applied biological sciences. Psychology
/ Hydrophobic and Hydrophilic Interactions
/ Membrane Proteins - chemistry
/ Membrane Proteins - classification
/ Membrane Proteins - metabolism
