5XGA

Crystal structure of the EnvZ periplasmic domain with CHAPS

「5DCJ」から置き換えられました

5XGA の概要

• エントリーDOI: 10.2210/pdb5xga/pdb
• 分子名称: Osmolarity sensor protein EnvZ, 3-[(3-CHOLAMIDOPROPYL)DIMETHYLAMMONIO]-1-PROPANESULFONATE, ACETIC ACID, ... (4 entities in total)
• 機能のキーワード: histidine kinase, envz, transferase
• 由来する生物種: Escherichia coli (strain K12)
• 細胞内の位置: Cell inner membrane; Multi-pass membrane protein: P0AEJ4
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15646.12

構造登録者

Hwang, E.,Cheong, H.K.,Jeon, Y.H.,Cheong, C. (登録日: 2017-04-13, 公開日: 2017-07-19, 最終更新日: 2024-03-27)

主引用文献

Hwang, E.,Cheong, H.K.,Kim, S.Y.,Kwon, O.,Blain, K.Y.,Choe, S.,Yeo, K.J.,Jung, Y.W.,Jeon, Y.H.,Cheong, C.
Crystal structure of the EnvZ periplasmic domain with CHAPS.
FEBS Lett., 591:1419-1428, 2017

PubMed Abstract: Bacteria sense and respond to osmolarity through the EnvZ-OmpR two-component system. The structure of the periplasmic sensor domain of EnvZ (EnvZ-PD) is not available yet. Here, we present the crystal structure of EnvZ-PD in the presence of CHAPS detergent. The structure of EnvZ-PD shows similar folding topology to the PDC domains of PhoQ, DcuS, and CitA, but distinct orientations of helices and β-hairpin structures. The CD and NMR spectra of EnvZ-PD in the presence of cholate, a major component of bile salts, are similar to those with CHAPS. Chemical cross-linking shows that the dimerization of EnvZ-PD is significantly inhibited by the CHAPS and cholate. Together with β-galactosidase assay, these results suggest that bile salts may affect the EnvZ structure and function in Escherichia coli.

PubMed: 28423182
DOI: 10.1002/1873-3468.12658

実験手法

X-RAY DIFFRACTION (1.951 Å)