Structural highlights
Function
[TAGH_BACSU] Part of the ABC transporter complex TagGH involved in teichoic acids export. Responsible for energy coupling to the transport system.[HAMAP-Rule:MF_01715][1]
Publication Abstract from PubMed
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.
Crystal structure of the N-terminal domain of TagH reveals a potential drug targeting site.,Yang CS, Huang WC, Ko TP, Wang YC, Wang AH, Chen Y Biochem Biophys Res Commun. 2021 Jan 15;536:1-6. doi: 10.1016/j.bbrc.2020.12.028., Epub 2020 Dec 22. PMID:33360015[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lazarevic V, Karamata D. The tagGH operon of Bacillus subtilis 168 encodes a two-component ABC transporter involved in the metabolism of two wall teichoic acids. Mol Microbiol. 1995 Apr;16(2):345-55. PMID:7565096
- ↑ Yang CS, Huang WC, Ko TP, Wang YC, Wang AH, Chen Y. Crystal structure of the N-terminal domain of TagH reveals a potential drug targeting site. Biochem Biophys Res Commun. 2021 Jan 15;536:1-6. doi: 10.1016/j.bbrc.2020.12.028., Epub 2020 Dec 22. PMID:33360015 doi:http://dx.doi.org/10.1016/j.bbrc.2020.12.028
