7DD0

Crystal structure of the N-terminal domain of TagH from Bacillus subtilis

Summary for 7DD0

• Entry DOI: 10.2210/pdb7dd0/pdb
• Descriptor: Teichoic acids export ATP-binding protein TagH (2 entities in total)
• Functional Keywords: abc transporter, atp-binding protein, transport protein, transprot protein, translocase
• Biological source: Bacillus subtilis subsp. subtilis str. 168
• Total number of polymer chains: 4
• Total formula weight: 128708.77

Authors

Ko, T.P.,Yang, C.S.,Wang, Y.C.,Chen, Y. (deposition date: 2020-10-27, release date: 2020-12-23, Last modification date: 2024-03-27)

Primary citation

Yang, C.S.,Huang, W.C.,Ko, T.P.,Wang, Y.C.,Wang, A.H.,Chen, Y.
Crystal structure of the N-terminal domain of TagH reveals a potential drug targeting site.
Biochem.Biophys.Res.Commun., 536:1-6, 2020

PubMed Abstract: 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.

PubMed: 33360015
DOI: 10.1016/j.bbrc.2020.12.028

Experimental method

X-RAY DIFFRACTION (2.7 Å)