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4R8C

Crystal Structure of CNG mimicking NaK-ETPP mutant in complex with Rb+

Summary for 4R8C
Entry DOI10.2210/pdb4r8c/pdb
Related3K0D 3K0G 4R50 4R6Z 4R7C 4R8B 4RAI 4RAR
DescriptorPotassium channel protein, RUBIDIUM ION, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (5 entities in total)
Functional Keywordsalpha helical membrane protein, chimera channel, transport protein
Biological sourceBacillus cereus ATCC 14579
Total number of polymer chains2
Total formula weight22752.94
Authors
De March, M.,Napolitano, L.M.R.,Onesti, S. (deposition date: 2014-09-01, release date: 2015-07-01, Last modification date: 2023-09-20)
Primary citationNapolitano, L.M.,Bisha, I.,De March, M.,Marchesi, A.,Arcangeletti, M.,Demitri, N.,Mazzolini, M.,Rodriguez, A.,Magistrato, A.,Onesti, S.,Laio, A.,Torre, V.
A structural, functional, and computational analysis suggests pore flexibility as the base for the poor selectivity of CNG channels.
Proc.Natl.Acad.Sci.USA, 112:E3619-E3628, 2015
Cited by
PubMed Abstract: Cyclic nucleotide-gated (CNG) ion channels, despite a significant homology with the highly selective K(+) channels, do not discriminate among monovalent alkali cations and are permeable also to several organic cations. We combined electrophysiology, molecular dynamics (MD) simulations, and X-ray crystallography to demonstrate that the pore of CNG channels is highly flexible. When a CNG mimic is crystallized in the presence of a variety of monovalent cations, including Na(+), Cs(+), and dimethylammonium (DMA(+)), the side chain of Glu66 in the selectivity filter shows multiple conformations and the diameter of the pore changes significantly. MD simulations indicate that Glu66 and the prolines in the outer vestibule undergo large fluctuations, which are modulated by the ionic species and the voltage. This flexibility underlies the coupling between gating and permeation and the poor ionic selectivity of CNG channels.
PubMed: 26100907
DOI: 10.1073/pnas.1503334112
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

226707

数据于2024-10-30公开中

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