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 PubMedBacterial 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
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This page was last modified 06:05, 20 January 2021.