7F2G

Crystal structure of the sensor domain of VbrK from Vibrio rotiferianus (crystal type 1)

7F2G の概要

• エントリーDOI: 10.2210/pdb7f2g/pdb
• 分子名称: Histidine kinase (2 entities in total)
• 機能のキーワード: sensor domain, beta-lactam antibiotic receptor, s-nitrosylation, signaling protein
• 由来する生物種: Vibrio rotiferianus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25115.64

構造登録者

Cho, S.Y.,Yoon, S.I. (登録日: 2021-06-11, 公開日: 2022-04-20, 最終更新日: 2024-10-16)

主引用文献

Cho, S.Y.,Yoon, S.I.
Crystal structure of the antibiotic- and nitrite-responsive histidine kinase VbrK sensor domain from Vibrio rotiferianus.
Biochem.Biophys.Res.Commun., 568:136-142, 2021

PubMed Abstract: Vibrio species are prevalent in the aquatic environments and can infect humans and aquatic organisms. Vibrio parahaemolyticus counteracts β-lactam antibiotics and enhances virulence using a regulation mechanism mediated by a two-component regulatory system (TCS) consisting of the VbrK histidine kinase and the VbrR response regulator. The periplasmic sensor domain of VbrK (VbrK) detects β-lactam antibiotics or undergoes S-nitrosylation in response to host nitrites. Although V. parahaemolyticus VbrK (vpVbrK) has recently been characterized through structural studies, it is unclear whether its structural features that are indispensable for biological functions are conserved in other VbrK orthologs. To structurally define the functionally critical regions of VbrK and address the structural dynamics of VbrK, we determined the crystal structures of Vibrio rotiferianus VbrK (vrVbrK) in two crystal forms and performed a comparative analysis of diverse VbrK structures. vrVbrK folds into a curved rod-shaped two-domain structure as observed in vpVbrK. The membrane-distal end of the vrVbrK structure, including the α3 helix and its neighboring loops, harbors both S-nitrosylation and antibiotic-sensing sites and displays high structural flexibility and diversity. Noticeably, the distal end is partially stabilized by a disulfide bond, which is formed by the cysteine residue that is S-nitrosylated in response to nitrite. Therefore, the distal end of VbrK plays a key role in initiating the VbrK-VbrR TCS pathway activation, and it is involved in the nitrosylation-mediated regulation of the structural dynamics of VbrK.

PubMed: 34214877
DOI: 10.1016/j.bbrc.2021.06.076

実験手法

X-RAY DIFFRACTION (1.9 Å)