4HDD

Domain swapping in the cytoplasmic domain of the Escherichia coli rhomboid protease

4HDD の概要

• エントリーDOI: 10.2210/pdb4hdd/pdb
• 関連するPDBエントリー: 2lep
• 分子名称: Rhomboid protease GlpG, ACETATE ION (3 entities in total)
• 機能のキーワード: domain swapping, peptidase, rhomboid protease, intramembrane protease, membrane, hydrolase
• 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: 1
• 化学式量合計: 9171.84

構造登録者

Lazareno-Saez, C.,Arutyunova, E.,Coquelle, N.,Lemieux, M.J. (登録日: 2012-10-02, 公開日: 2013-02-06, 最終更新日: 2024-10-30)

主引用文献

Lazareno-Saez, C.,Arutyunova, E.,Coquelle, N.,Lemieux, M.J.
Domain swapping in the cytoplasmic domain of the Escherichia coli rhomboid protease.
J.Mol.Biol., 425:1127-1142, 2013

PubMed Abstract: Rhomboids are membrane-embedded serine proteases that cleave membrane protein substrates. Escherichia coli rhomboid GlpG (ecGlpG) consists of an N-terminal cytoplasmic domain and a membrane domain containing the active site. We determined the crystal structure of the soluble cytoplasmic domain of ecGlpG at 1.35Å resolution and examined whether this domain affected the catalytic activity of the enzyme. The structure revealed that the ecGlpG cytoplasmic domain exists as a dimer with extensive domain swapping between the two monomers. Domain-swapped dimers can be isolated from the full-length protein, suggesting that this is a physiologically relevant structure. An extensive steady-state kinetic analysis of the full-length ecGlpG and its membrane domain using soluble and transmembrane model protein substrates resulted in an unexpected conclusion: removal of the cytoplasmic domain does not alter the catalytic parameters for detergent-solubilized rhomboid for both substrates.

PubMed: 23353827
DOI: 10.1016/j.jmb.2013.01.019

実験手法

X-RAY DIFFRACTION (1.35 Å)