2MJ6

Solution structure of the extracellular sensor domain of DraK histidine kinase

2MJ6 の概要

• エントリーDOI: 10.2210/pdb2mj6/pdb
• NMR情報: BMRB: 19707
• 分子名称: Putative two-component system histidine kinase (1 entity in total)
• 機能のキーワード: drak, histidine kinase, transferase
• 由来する生物種: Streptomyces coelicolor
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9760.80

構造登録者

Yeo, K.,Cheong, H. (登録日: 2013-12-25, 公開日: 2014-09-24, 最終更新日: 2024-05-15)

主引用文献

Yeo, K.J.,Hong, Y.S.,Jee, J.G.,Lee, J.K.,Kim, H.J.,Park, J.W.,Kim, E.H.,Hwang, E.,Kim, S.Y.,Lee, E.G.,Kwon, O.,Cheong, H.K.
Mechanism of the pH-Induced Conformational Change in the Sensor Domain of the DraK Histidine Kinase via the E83, E105, and E107 Residues
Plos One, 9:e107168-e107168, 2014

PubMed Abstract: The DraR/DraK two-component system was found to be involved in the differential regulation of antibiotic biosynthesis in a medium-dependent manner; however, its function and signaling and sensing mechanisms remain unclear. Here, we describe the solution structure of the extracellular sensor domain of DraK and suggest a mechanism for the pH-dependent conformational change of the protein. The structure contains a mixed alpha-beta fold, adopting a fold similar to the ubiquitous sensor domain of histidine kinase. A biophysical study demonstrates that the E83, E105, and E107 residues have abnormally high pKa values and that they drive the pH-dependent conformational change for the extracellular sensor domain of DraK. We found that a triple mutant (E83L/E105L/E107A) is pH independent and mimics the low pH structure. An in vivo study showed that DraK is essential for the recovery of the pH of Streptomyces coelicolor growth medium after acid shock. Our findings suggest that the DraR/DraK two-component system plays an important role in the pH regulation of S. coelicolor growth medium. This study provides a foundation for the regulation and the production of secondary metabolites in Streptomyces.

PubMed: 25203403
DOI: 10.1371/journal.pone.0107168

実験手法

SOLUTION NMR