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Article
Nature Structural & Molecular Biology - 13, 1084 - 1091 (2006)
Published online: 10 November 2006; | doi:10.1038/nsmb1179

Structural analysis of a rhomboid family intramembrane protease reveals a gating mechanism for substrate entry

Zhuoru Wu1, 4, Nieng Yan1, 4, Liang Feng1, 4, Adam Oberstein1, Hanchi Yan1, Rosanna P Baker2, Lichuan Gu3, Philip D Jeffrey1, Sinisa Urban2 & Yigong Shi1

1  Department of Molecular Biology, Lewis Thomas Laboratory, Princeton University, Princeton, New Jersey 08544, USA.

2  Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.

3  State Key Laboratory of Microbial Technology, Shandong University, Jinan 250100, China.

4  These authors contributed equally to this work.

Correspondence should be addressed to Yigong Shi ygshi@princeton.edu

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 Å 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.

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Nature Structural & Molecular Biology
ISSN: 1545-9993
EISSN: 1545-9985
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