Crystal structure of the N-terminal domain of TagH reveals a potential drug targeting site
| Autor: | Andrew H.-J. Wang, Yeh Chen, Chia-Shin Yang, Tzu Ping Ko, Wei Chien Huang, Yu-Chuan Wang |
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| Rok vydání: | 2021 |
| Předmět: |
Models
Molecular 0301 basic medicine Hydrolases Stereochemistry Dimer ATPase Biophysics ATP-binding cassette transporter Crystallography X-Ray Biochemistry 03 medical and health sciences chemistry.chemical_compound Adenosine Triphosphate Drug Delivery Systems 0302 clinical medicine Bacterial Proteins Amino Acid Sequence Binding site Molecular Biology Teichoic acid Diphosphonates biology Transporter Cell Biology Transmembrane protein Kinetics 030104 developmental biology chemistry Targeted drug delivery 030220 oncology & carcinogenesis biology.protein ATP-Binding Cassette Transporters |
| Zdroj: | Biochemical and Biophysical Research Communications. 536:1-6 |
| ISSN: | 0006-291X |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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