| People | Locations | Statistics |
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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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Arleth, Lise
University of Copenhagen
in Cooperation with on an Cooperation-Score of 37%
Topics
Publications (15/15 displayed)
- 2023Modeling of flexible membrane-bound biomolecular complexes for solution small-angle scatteringcitations
- 2023Aggregative adherence fimbriae form compact structures as seen by SAXScitations
- 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
- 2021Mg2+-dependent conformational equilibria in CorA: an integrated view on transport regulation
- 2021The microscopic distribution of hydrophilic polymers in interpenetrating polymer networks (IPNs) of medical grade siliconecitations
- 2020Assessment of structure factors for analysis of small-angle scattering data from desired or undesired aggregatescitations
- 2020Dispersion state of TiO2 pigment particles studied by ultra-small-angle X-ray scattering revealing dependence on dispersant but limited change during drying of paint coatingcitations
- 2019Circularized and solubility-enhanced MSPs facilitate simple and high-yield production of stable nanodiscs for studies of membrane proteins in solutioncitations
- 2016Construction of insulin 18-mer nanoassemblies driven by coordination to Iron(II) and Zinc(II) ions at distinct sitescitations
- 2016Dimeric peptides with three different linkers self-assemble with phospholipids to form peptide nanodiscs that stabilize membrane proteinscitations
- 2015Small-angle scattering determination of the shape and localization of human cytochrome P450 embedded in a phospholipid nanodisc environmentcitations
- 2014Stealth carriers for low-resolution structure determination of membrane proteins in solutioncitations
- 2013Self-assembly of designed coiled coil peptides studied by small-angle X-ray scattering and analytical ultracentrifugationcitations
- 2013WillItFitcitations
Places of action
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article
Mg2+-dependent conformational equilibria in CorA and an integrated view on transport regulation
Abstract
<p>The CorA family of proteins regulates the homeostasis of divalent metal ions in many bacteria, archaea, and eukaryotic mitochondria, making it an important target in the investigation of the mechanisms of transport and its functional regulation. Although numerous structures of open and closed channels are now available for the CorA family, the mechanism of the transport regulation remains elusive. Here, we investigated the conformational distribution and associated dynamic behaviour of the pentameric Mg2+ channel CorA at room temperature using small-angle neutron scattering (SANS) in combination with molecular dynamics (MD) simulations and solid-state nuclear magnetic resonance spectroscopy (NMR). We find that neither the Mg2+-bound closed structure nor the Mg2+-free open forms are sufficient to explain the average conformation of CorA. Our data support the presence of conformational equilibria between multiple states, and we further find a variation in the behaviour of the backbone dynamics with and without Mg2+. We propose that CorA must be in a dynamic equilibrium between different non-conducting states, both symmetric and asymmetric, regardless of bound Mg2+ but that conducting states become more populated in Mg2+-free conditions. These properties are regulated by backbone dynamics and are key to understanding the functional regulation of CorA.</p>