2IC8

Crystal structure of GlpG

Summary for 2IC8

• Entry DOI: 10.2210/pdb2ic8/pdb
• Descriptor: Protein glpG, nonyl beta-D-glucopyranoside (3 entities in total)
• Functional Keywords: rhomboid, intramembrane proteolysis, membrane protein
• Biological source: Escherichia coli
• Cellular location: Cell inner membrane; Multi-pass membrane protein: P09391
• Total number of polymer chains: 1
• Total formula weight: 24205.05

Authors

Ha, Y. (deposition date: 2006-09-12, release date: 2006-10-17, Last modification date: 2024-02-21)

Primary citation

Wang, Y.,Zhang, Y.,Ha, Y.
Crystal structure of a rhomboid family intramembrane protease.
Nature, 444:179-180, 2006

PubMed Abstract: 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.

PubMed: 17051161
DOI: 10.1038/nature05255

Experimental method

X-RAY DIFFRACTION (2.1 Å)