Crystal structure of the N-terminal domain of TagH reveals a potential drug targeting site

Chia Shin Yang, Wei Chien Huang, Tzu Ping Ko, Yu Chuan Wang, Andrew H.J. Wang, Yeh Chen

研究成果: 雜誌貢獻文章同行評審

摘要

Bacterial wall teichoic acids (WTAs) are synthesized intracellularly and exported by a two-component transporter, TagGH, comprising the transmembrane and ATPase subunits TagG and TagH. Here the dimeric structure of the N-terminal domain of TagH (TagH-N) was solved by single-wavelength anomalous diffraction using a selenomethionine-containing crystal, which shows an ATP-binding cassette (ABC) architecture with RecA-like and helical subdomains. Besides significant structural differences from other ABC transporters, a prominent patch of positively charged surface is seen in the center of the TagH-N dimer, suggesting a potential binding site for the glycerol phosphate chain of WTA. The ATPase activity of TagH-N was inhibited by clodronate, a bisphosphonate, in a non-competitive manner, consistent with the proposed WTA-binding site for drug targeting.

原文英語
頁(從 - 到)1-6
頁數6
期刊Biochemical and Biophysical Research Communications
536
DOIs
出版狀態已發佈 - 1月 15 2021
對外發佈

ASJC Scopus subject areas

  • 生物物理學
  • 生物化學
  • 分子生物學
  • 細胞生物學

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