2XTV

Structure of E.coli rhomboid protease GlpG, active site mutant, S201T, orthorhombic crystal form

2XTV の概要

• エントリーDOI: 10.2210/pdb2xtv/pdb
• 関連するPDBエントリー: 2IC8 2IRV 2XOV 2XOW 2XTU
• 分子名称: RHOMBOID PROTEASE GLPG, 1,2-DIMYRISTOYL-RAC-GLYCERO-3-PHOSPHOCHOLINE (3 entities in total)
• 機能のキーワード: hydrolase, membrane protein
• 由来する生物種: ESCHERICHIA COLI
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29747.10

構造登録者

Vinothkumar, K.R. (登録日: 2010-10-12, 公開日: 2011-02-02, 最終更新日: 2023-12-20)

主引用文献

Vinothkumar, K.R.
Structure of rhomboid protease in a lipid environment.
J. Mol. Biol., 407:232-247, 2011

PubMed Abstract: Structures of the prokaryotic homologue of rhomboid proteases reveal a core of six transmembrane helices, with the active-site residues residing in a hydrophilic cavity. The native environment of rhomboid protease is a lipid bilayer, yet all the structures determined thus far are in a nonnative detergent environment. There remains a possibility of structural artefacts arising from the use of detergents. In an attempt to address the effect of detergents on the structure of rhomboid protease, crystals of GlpG, an Escherichia coli rhomboid protease in a lipid environment, were obtained using two alternative approaches. The structure of GlpG refined to 1. 7-Å resolution was obtained from crystals grown in the presence of lipid bicelles. This structure reveals well-ordered and partly ordered lipid molecules forming an annulus around the protein. Lipid molecules adapt to the surface features of protein and arrange such that they match the hydrophobic thickness of GlpG. Virtually identical two-dimensional crystals were also obtained after detergent removal by dialysis. A comparison of an equivalent structure determined in a completely delipidated detergent environment provides insights on how detergent substitutes for lipid. A detergent molecule is also observed close to the active site, helping to postulate a model for substrate binding and hydrolysis in rhomboids.

PubMed: 21256137
DOI: 10.1016/j.jmb.2011.01.029

実験手法

X-RAY DIFFRACTION (1.7 Å)