Hydrogen-deuterium exchange mass spectrometry captures distinct dynamics upon substrate and inhibitor binding to a transporter
| Autor: | Ruyu Jia, Chloe Martens, Mrinal Shekhar, Shashank Pant, Grant A. Pellowe, Andy M. Lau, Heather E. Findlay, Nicola J. Harris, Emad Tajkhorshid, Paula J. Booth, Argyris Politis |
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| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: | |
| Zdroj: | Nature Communications, Vol 11, Iss 1, Pp 1-10 (2020) |
| Druh dokumentu: | article |
| ISSN: | 2041-1723 84323884 |
| DOI: | 10.1038/s41467-020-20032-3 |
| Popis: | XylE is a bacterial xylose transporter and homologue of human glucose transporters GLUTs 1-4. HDX-MS, mutagenesis and MD simulations suggest that protonation of a conserved aspartate triggers conformational transition from outward- to inward facing state only in the presence of substrate xylose. In contrast, inhibitor glucose locks the transporter in the outward facing state. |
| Databáze: | Directory of Open Access Journals |
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