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Cryo-EM structure of CorA in complex with conformation-specific synthetic antibody C18 and 100 uM MgCl2


ABSTRACT:

SUBMITTER: Satchal Krishna Erramilli 

PROVIDER: EMPIAR-12500 | biostudies-other |

REPOSITORIES: biostudies-other

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Conformational ensembles of the magnesium channel CorA reveal structural basis for channel gating.

Erramilli Satchal K SK   Nosol Kamil K   Pietrzak-Lichwa Krzysztof K   Schmandt Nicolaus N   Li Tian T   Tokarz Piotr P   Hou Jingkai J   Zhao Minglei M   Perozo Eduardo E   Kossiakoff Anthony A AA  

Proceedings of the National Academy of Sciences of the United States of America 20260217 8


In prokaryotes, CorA is the primary influx pathway for magnesium, a critical divalent cation in cellular physiology and biochemistry. Mechanistic studies show that homopentameric CorA is regulated through an intracellular [Mg<sup>2+</sup>]-dependent negative feedback loop, involving the asymmetric participation of individual subunits. To understand the connection between asymmetry and activation, we used single-particle cryo-EM to solve sixteen structures of nanodisc-reconstituted CorA. We utili  ...[more]

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