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| Naji, M. |
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| Motta, Antonella |
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| Aletan, Dirar |
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| Mohamed, Tarek |
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| Ertürk, Emre |
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| Taccardi, Nicola |
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| Kononenko, Denys |
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| Petrov, R. H. | Madrid |
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| Alshaaer, Mazen | Brussels |
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| Bih, L. |
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| Casati, R. |
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| Muller, Hermance |
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| Kočí, Jan | Prague |
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| Šuljagić, Marija |
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| Kalteremidou, Kalliopi-Artemi | Brussels |
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| Azam, Siraj |
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| Ospanova, Alyiya |
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| Blanpain, Bart |
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| Ali, M. A. |
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| Popa, V. |
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| Rančić, M. |
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| Ollier, Nadège |
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| Azevedo, Nuno Monteiro |
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| Landes, Michael |
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| Rignanese, Gian-Marco |
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Martel, Anne
Institut Laue-Langevin
in Cooperation with on an Cooperation-Score of 37%
Topics
Publications (12/12 displayed)
- 2022Mg2+-dependent conformational equilibria in CorA and an integrated view on transport regulationcitations
- 2022Mg2+-dependent conformational equilibria in CorA and an integrated view on transport regulationcitations
- 2022Small-angle x-ray and neutron scattering of MexR and its complex with DNA supports a conformational selection binding model.citations
- 2022A round-robin approach provides a detailed assessment of biomolecular small-angle scattering data reproducibility and yields consensus curves for benchmarkingcitations
- 2022A round-robin approach provides a detailed assessment of biomolecular small-angle scattering data reproducibility and yields consensus curves for benchmarkingcitations
- 2021Interpenetrated biosurfactant-silk fibroin networks – a SANS studycitations
- 2021Pepsi-SAXS/SANS -small-angle scattering-guided tools for integrative structural bioinformaticscitations
- 2021Mg2+-dependent conformational equilibria in CorA: an integrated view on transport regulation
- 2020Hemicellulose binding and the spacing of cellulose microfibrils in spruce woodcitations
- 2017Fast Collisional Lipid Transfer Among Polymer-Bounded Nanodiscs.citations
- 2016Dimeric peptides with three different linkers self-assemble with phospholipids to form peptide nanodiscs that stabilize membrane proteinscitations
- 2015Large-Scale Conformational Dynamics Control H5N1 Influenza Polymerase PB2 Binding to Importin α.citations
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article
Large-Scale Conformational Dynamics Control H5N1 Influenza Polymerase PB2 Binding to Importin α.
Abstract
Influenza A RNA polymerase complex is formed from three components, PA, PB1, and PB2. PB2 is independently imported into the nucleus prior to polymerase reconstitution. All crystallographic structures of the PB2 C-terminus (residues 536-759) reveal two globular domains, 627 and NLS, that form a tightly packed heterodimer. The molecular basis of the affinity of 627-NLS for importins remained unclear from these structures, apparently requiring large-scale conformational changes prior to importin binding. Using a combination of solution-state NMR, small-angle neutron scattering, small-angle X-ray scattering (SAXS), and Förster resonance energy transfer (FRET), we show that 627-NLS populates a temperature-dependent dynamic equilibrium between closed and open states. The closed state is stabilized by a tripartite salt bridge involving the 627-NLS interface and the linker, that becomes flexible in the open state, with 627 and NLS dislocating into a highly dynamic ensemble. Activation enthalpies and entropies associated with the rupture of this interface were derived from simultaneous analysis of temperature-dependent chemical exchange saturation transfer measurements, revealing a strong temperature dependence of both open-state population and exchange rate. Single-molecule FRET and SAXS demonstrate that only the open-form is capable of binding to importin α and that, upon binding, the 627 domain samples a dynamic conformational equilibrium in the vicinity of the C-terminus of importin α. This intrinsic large-scale conformational flexibility therefore enables 627-NLS to bind importin through conformational selection from a temperature-dependent equilibrium comprising both functional forms of the protein.