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3R65

MthK channel pore E92Q mutant

Summary for 3R65
Entry DOI10.2210/pdb3r65/pdb
Related3LDC
DescriptorCalcium-gated potassium channel mthK, POTASSIUM ION (3 entities in total)
Functional Keywordstrans-membrane, ion channel, potassium ion, membrane, membrane protein
Biological sourceMethanothermobacter thermautotrophicus str. Delta H
Cellular locationCell membrane; Multi-pass membrane protein: O27564
Total number of polymer chains1
Total formula weight9189.99
Authors
Shi, N.,Zeng, W.,Ye, S.,Li, Y.,Jiang, Y. (deposition date: 2011-03-21, release date: 2012-02-01, Last modification date: 2023-09-13)
Primary citationShi, N.,Zeng, W.,Ye, S.,Li, Y.,Jiang, Y.
Crucial points within the pore as determinants of K+ channel conductance and gating
J.Mol.Biol., 411:27-35, 2011
Cited by
PubMed Abstract: While selective for K⁺, K⁺ channels vary significantly among their rate of ion permeation. Here, we probe the effect of steric hindrance and electrostatics within the ion conduction pathway on K⁺ permeation in the MthK K⁺ channel using structure-based mutagenesis combined with single-channel electrophysiology and X-ray crystallography. We demonstrate that changes in side-chain size and polarity at Ala88, which forms the constriction point of the open MthK pore, have profound effects on single-channel conductance as well as open probability. We also reveal that the negatively charged Glu92s at the intracellular entrance of the open pore form an electrostatic trap, which stabilizes a hydrated K⁺ and facilitates ion permeation. This electrostatic attraction is also responsible for intracellular divalent blockage, which renders the channel inward rectified in the presence of Ca²⁺. In light of the high structural conservation of the selectivity filter, the size and chemical environment differences within the portion of the ion conduction pathway other than the filter are likely the determinants for the conductance variations among K⁺ channels.
PubMed: 21554888
DOI: 10.1016/j.jmb.2011.04.058
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

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