Tantirimudalige, Sarala and Buckley, Theresa Sophia Claire and Chandramohan, Arun and Richter, Rebecca Michaela and Ziegler, Christine and Anand, Ganesh S. (2022) Hyperosmotic Stress Allosterically Reconfigures Betaine Binding Pocket in BetP. JOURNAL OF MOLECULAR BIOLOGY, 434 (17): 167747. ISSN 0022-2836, 1089-8638
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The transporter BetP in C. glutamicum is essential in maintaining bacterial cell viability during hyperosmotic stress and functions by co-transporting betaine and Na+ into bacterial cells. Hyperosmotic stress leads to increased intracellular K+ concentrations which in turn promotes betaine binding. While structural details of multiple end state conformations of BetP have provided high resolution snapshots, how K+ sensing by the C-terminal domain is allosterically relayed to the betaine binding site is not well understood. In this study, we describe conformational dynamics in solution of BetP using amide hydrogen/deuterium exchange mass spectrometry. These reveal how K+ alters conformation of the disordered C- and N-terminal domains to allosterically reconfigure transmembrane helices 3, 8, and 10 to enhance betaine interactions. A map of the betaine binding site, at near single amino acid resolution, reveals a critical extrahelical H-bond mediated by TM3 with betaine. (C) 2022 Elsevier Ltd. All rights reserved.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | CORYNEBACTERIUM-GLUTAMICUM; ORGANIC OSMOLYTES; TRANSPORTER BETP; MOLECULAR-BASIS; CARRIER BETP; BACTERIA; SPECIFICITY; PRECURSOR; EXCHANGE; SYSTEM; |
| Subjects: | 500 Science > 550 Earth sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Christine Ziegler |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 01 Feb 2024 06:31 |
| Last Modified: | 01 Feb 2024 06:31 |
| URI: | https://pred.uni-regensburg.de/id/eprint/57838 |
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