2NRF

Crystal Structure of GlpG, a Rhomboid family intramembrane protease

2NRF の概要

• エントリーDOI: 10.2210/pdb2nrf/pdb
• 分子名称: Protein GlpG (2 entities in total)
• 機能のキーワード: integral membrane protein, membrane protein
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell inner membrane ; Multi-pass membrane protein : P09391
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 41056.62

構造登録者

Wu, Z.,Yan, N.,Feng, L.,Yan, H.,Gu, L.,Shi, Y. (登録日: 2006-11-02, 公開日: 2006-11-14, 最終更新日: 2023-08-30)

主引用文献

Wu, Z.,Yan, N.,Feng, L.,Oberstein, A.,Yan, H.,Baker, R.P.,Gu, L.,Jeffrey, P.D.,Urban, S.,Shi, Y.
Structural analysis of a rhomboid family intramembrane protease reveals a gating mechanism for substrate entry.
Nat.Struct.Mol.Biol., 13:1084-1091, 2006

PubMed Abstract: 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.

PubMed: 17099694
DOI: 10.1038/nsmb1179

実験手法

X-RAY DIFFRACTION (2.6 Å)