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

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish
Pages (from-to)1-6
Number of pages6
JournalBiochemical and Biophysical Research Communications
Publication statusPublished - Jan 15 2021
Externally publishedYes


  • ABC transporter
  • Bisphosphonates
  • Drug discovery
  • Wall teichoic acids

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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