@article{168496,
  keywords = {Animals, Models, Molecular, Water, Crystallography, X-Ray, Protein Structure, Tertiary, Humans, Escherichia coli, Molecular Sequence Data, Binding Sites, Substrate Specificity, Membrane Proteins, Amino Acid Sequence, Escherichia coli Proteins, Sequence Alignment, Cell Membrane, Conserved Sequence, Protein Structure, Secondary, DNA-Binding Proteins, Endopeptidases, Structural Homology, Protein},
  author = {Zhuoru Wu and Nieng Yan and Liang Feng and Adam Oberstein and Hanchi Yan and Rosanna Baker and Lichuan Gu and Philip Jeffrey and Sinisa Urban and Yigong Shi},
  title = {Structural analysis of a rhomboid family intramembrane protease reveals a gating mechanism for substrate entry},
  abstract = {<p>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 alpha4 approximately 10 A 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 alpha5 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 alpha5.</p>
},
  year = {2006},
  journal = {Nat Struct Mol Biol},
  volume = {13},
  pages = {1084-91},
  month = {12/2006},
  issn = {1545-9993},
  doi = {10.1038/nsmb1179},
  language = {eng},
}