- EMDB-13326: T. maritima CorA in DDM micelles without Mg2+ bound in D2O -
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Basic information
Entry
Database: EMDB / ID: EMD-13326
Title
T. maritima CorA in DDM micelles without Mg2+ bound in D2O
Map data
T. maritima CorA in DDM micelles without Mg2 bound (in EDTA).
Sample
Complex: CorA pentamer without Mg2+ bound
Protein or peptide: Thermotoga maritima CorA
Function / homology
Function and homology information
magnesium ion transmembrane transport / cobalt ion transport / cobalt ion transmembrane transporter activity / magnesium ion transmembrane transporter activity / cobalt ion binding / protein homooligomerization / magnesium ion binding / identical protein binding / plasma membrane Similarity search - Function
Magnesium/cobalt transport protein CorA / CorA, cytoplasmic domain / CorA, transmembrane region / Mg2+ transporter protein, CorA-like/Zinc transport protein ZntB / CorA-like Mg2+ transporter protein Similarity search - Domain/homology
Journal: Elife / Year: 2022 Title: Mg-dependent conformational equilibria in CorA and an integrated view on transport regulation. Authors: Nicolai Tidemand Johansen / Marta Bonaccorsi / Tone Bengtsen / Andreas Haahr Larsen / Frederik Grønbæk Tidemand / Martin Cramer Pedersen / Pie Huda / Jens Berndtsson / Tamim Darwish / ...Authors: Nicolai Tidemand Johansen / Marta Bonaccorsi / Tone Bengtsen / Andreas Haahr Larsen / Frederik Grønbæk Tidemand / Martin Cramer Pedersen / Pie Huda / Jens Berndtsson / Tamim Darwish / Nageshewar Rao Yepuri / Anne Martel / Thomas Günther Pomorski / Andrea Bertarello / Mark Sansom / Mikaela Rapp / Ramon Crehuet / Tobias Schubeis / Kresten Lindorff-Larsen / Guido Pintacuda / Lise Arleth / Abstract: 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 ...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 Mg 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 Mg-bound closed structure nor the Mg-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 Mg. We propose that CorA must be in a dynamic equilibrium between different non-conducting states, both symmetric and asymmetric, regardless of bound Mg but that conducting states become more populated in Mg-free conditions. These properties are regulated by backbone dynamics and are key to understanding the functional regulation of CorA.
History
Deposition
Aug 4, 2021
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Header (metadata) release
Feb 23, 2022
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Map release
Feb 23, 2022
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Update
Feb 23, 2022
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Current status
Feb 23, 2022
Processing site: PDBe / Status: Released
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Structure visualization
Movie
Surface view with section colored by density value
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