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. Author manuscript; available in PMC: 2009 Aug 1.
Published in final edited form as: Biol Chem. 2008 Aug;389(8):1107–1115. doi: 10.1515/BC.2008.122

Figure 1. Structure and gating models of the GlpG rhomboid protease from Escherichia coli.

Figure 1

A. The ‘front view’ of the core domain of GlpG is shown laterally from the plane of the membrane, with the extracellular side up and the cytosolic side down. The membrane-submerged L1 loop is highlighted in black, and the hypothetical conformation change to allow substrate access between transmembrane helices 1 and 3 is depicted by an upward arrow. B. The ‘back view’ of the GlpG protease is shown laterally as above, with the transmembrane helix 5 highlighted in black. The open conformation is shown (coordinates from PDB N2RF), with an arrow depicting the proposed transmembrane segment 5 tilting and Cap movement that gates substrate access to the active site serine (in black ball-and-stick).