Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 13, Issue 12, Pages 1084-1091Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb1179
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Funding
- NIAID NIH HHS [1R01AI066025] Funding Source: Medline
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Intramembrane proteolysis regulates diverse biological processes. Cleavage of substrate peptide bonds within the membrane bilayer is catalyzed by integral membrane proteases. Here we report the crystal structure of the transmembrane core domain of GlpG, a rhomboid-family intramembrane serine protease from Escherichia coli. The protein contains six transmembrane helices, with the catalytic Ser201 located at the N terminus of helix alpha 4 approximately 10 angstrom below the membrane surface. Access to water molecules is provided by a central cavity that opens to the extracellular region and converges on Ser201. One of the two GlpG molecules in the asymmetric unit has an open conformation at the active site, with the transmembrane helix alpha 5 bent away from the rest of the molecule. Structural analysis suggests that substrate entry to the active site is probably gated by the movement of helix alpha 5.
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