Structure, function, and ion-binding properties of a K+ channel stabilized in the 2,4-ion-bound configuration

Proceedings of the National Academy of Sciences of the United States of America
Cholpon TilegenovaLuis G Cuello

Abstract

Here, we present the atomic resolution crystallographic structure, the function, and the ion-binding properties of the KcsA mutants, G77A and G77C, that stabilize the 2,4-ion-bound configuration (i.e., water, K+, water, K+-ion-bound configuration) of the K+ channel's selectivity filter. A full functional and thermodynamic characterization of the G77A mutant revealed wild-type-like ion selectivity and apparent K+-binding affinity, in addition to showing a lack of C-type inactivation gating and a marked reduction in its single-channel conductance. These structures validate, from a structural point of view, the notion that 2 isoenergetic ion-bound configurations coexist within a K+ channel's selectivity filter, which fully agrees with the water-K+-ion-coupled transport detected by streaming potential measurements.

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Citations

Mar 11, 2020·Annual Review of Physical Chemistry·Mangesh I ChaudhariSusan B Rempe
Jun 11, 2020·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Anthony LewisSteve A N Goldstein
Jan 26, 2020·Proceedings of the National Academy of Sciences of the United States of America·Williams E MirandaSergei Yu Noskov
Dec 19, 2020·Computational and Structural Biotechnology Journal·Dai-Lin LiChin-Ling Chen
Mar 21, 2021·Proceedings of the National Academy of Sciences of the United States of America·Kenichiro MitaShigetoshi Oiki
Apr 24, 2021·Journal of Molecular Biology·Andrei MironenkoWojciech Kopec
May 21, 2021·The Journal of General Physiology·Tibor G SzantoGyorgy Panyi
Jun 12, 2021·Physical Review Letters·W A T GibbyP V E McClintock
Jul 15, 2021·Chemical Science·Zhifeng JingPengyu Ren

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