6eo1

The electron crystallography structure of the cAMP-bound potassium channel MloK1 (PCO-refined)The electron crystallography structure of the cAMP-bound potassium channel MloK1 (PCO-refined)

Structural highlights

6eo1 is a 4 chain structure with sequence from Mesorhizobium japonicum MAFF 303099. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron crystallography, Resolution 4.5Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CNGK1_RHILO Cyclic nucleotide-regulated potassium channel activated by cAMP.^[1]

Publication Abstract from PubMed

Eukaryotic cyclic nucleotide-modulated channels perform their diverse physiological roles by opening and closing their pores to ions in response to cyclic nucleotide binding. We here present a structural model for the cyclic nucleotide-modulated potassium channel homolog from Mesorhizobium loti, MloK1, determined from 2D crystals in the presence of lipids. Even though crystals diffract electrons to only approximately 10 A, using cryoelectron microscopy (cryo-EM) and recently developed computational methods, we have determined a 3D map of full-length MloK1 in the presence of cyclic AMP (cAMP) at approximately 4.5 A isotropic 3D resolution. The structure provides a clear picture of the arrangement of the cyclic nucleotide-binding domains with respect to both the pore and the putative voltage sensor domains when cAMP is bound, and reveals a potential gating mechanism in the context of the lipid-embedded channel.

High-Resolution Cryoelectron Microscopy Structure of the Cyclic Nucleotide-Modulated Potassium Channel MloK1 in a Lipid Bilayer.,Kowal J, Biyani N, Chami M, Scherer S, Rzepiela AJ, Baumgartner P, Upadhyay V, Nimigean CM, Stahlberg H Structure. 2017 Dec 1. pii: S0969-2126(17)30365-9. doi:, 10.1016/j.str.2017.11.012. PMID:29249605^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Clayton GM, Silverman WR, Heginbotham L, Morais-Cabral JH. Structural basis of ligand activation in a cyclic nucleotide regulated potassium channel. Cell. 2004 Nov 24;119(5):615-27. PMID:15550244 doi:10.1016/j.cell.2004.10.030
↑ Kowal J, Biyani N, Chami M, Scherer S, Rzepiela AJ, Baumgartner P, Upadhyay V, Nimigean CM, Stahlberg H. High-Resolution Cryoelectron Microscopy Structure of the Cyclic Nucleotide-Modulated Potassium Channel MloK1 in a Lipid Bilayer. Structure. 2017 Dec 1. pii: S0969-2126(17)30365-9. doi:, 10.1016/j.str.2017.11.012. PMID:29249605 doi:http://dx.doi.org/10.1016/j.str.2017.11.012

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OCA

[1] Clayton GM, Silverman WR, Heginbotham L, Morais-Cabral JH. Structural basis of ligand activation in a cyclic nucleotide regulated potassium channel. Cell. 2004 Nov 24;119(5):615-27. PMID:15550244 doi:10.1016/j.cell.2004.10.030

[2] Kowal J, Biyani N, Chami M, Scherer S, Rzepiela AJ, Baumgartner P, Upadhyay V, Nimigean CM, Stahlberg H. High-Resolution Cryoelectron Microscopy Structure of the Cyclic Nucleotide-Modulated Potassium Channel MloK1 in a Lipid Bilayer. Structure. 2017 Dec 1. pii: S0969-2126(17)30365-9. doi:, 10.1016/j.str.2017.11.012. PMID:29249605 doi:http://dx.doi.org/10.1016/j.str.2017.11.012

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