1a:I[76865,["/_next/static/chunks/d07a36b34c614bac.js","/_next/static/chunks/a439560253821848.js","/_next/static/chunks/992d80515d7f780d.js","/_next/static/chunks/3adfb55b15c8d19c.js","/_next/static/chunks/b642b3e65e2c6231.js","/_next/static/chunks/fc50eca1ad01dc11.js","/_next/static/chunks/afc6bdd59b458409.js","/_next/static/chunks/6448cccc5d968256.js"],"Grid"] 1b:I[17291,["/_next/static/chunks/d07a36b34c614bac.js","/_next/static/chunks/a439560253821848.js","/_next/static/chunks/992d80515d7f780d.js","/_next/static/chunks/3adfb55b15c8d19c.js","/_next/static/chunks/b642b3e65e2c6231.js","/_next/static/chunks/fc50eca1ad01dc11.js","/_next/static/chunks/afc6bdd59b458409.js","/_next/static/chunks/6448cccc5d968256.js"],"GridCol"] 1c:I[34616,["/_next/static/chunks/d07a36b34c614bac.js","/_next/static/chunks/a439560253821848.js","/_next/static/chunks/992d80515d7f780d.js","/_next/static/chunks/3adfb55b15c8d19c.js","/_next/static/chunks/b642b3e65e2c6231.js","/_next/static/chunks/fc50eca1ad01dc11.js","/_next/static/chunks/afc6bdd59b458409.js","/_next/static/chunks/6448cccc5d968256.js"],"Avatar"] 1d:I[32972,["/_next/static/chunks/d07a36b34c614bac.js","/_next/static/chunks/a439560253821848.js","/_next/static/chunks/992d80515d7f780d.js","/_next/static/chunks/3adfb55b15c8d19c.js","/_next/static/chunks/b642b3e65e2c6231.js","/_next/static/chunks/fc50eca1ad01dc11.js","/_next/static/chunks/afc6bdd59b458409.js","/_next/static/chunks/6448cccc5d968256.js"],"default"] 1e:T449,Voltage-dependent Ca²⁺ channels (Cavs) are indispensable for coupling action potentials with Ca²⁺ signaling in living organisms. The structure of Cavs is similar to that of voltage-dependent Na⁺ channels (Navs). It is known that prokaryotic Navs can obtain Ca²⁺ selectivity by negative charge mutations of the selectivity filter, but native prokaryotic Cavs had not yet been identified. We report the first identification of a native prokaryotic Cav, CavMr, whose selectivity filter contains a smaller number of negatively charged residues than that of artificial prokaryotic Cavs. A relative mutant whose selectivity filter was replaced with that of CavMr exhibits high Ca²⁺ selectivity. Mutational analyses revealed that the glycine residue of the CavMr selectivity filter is a determinant for Ca²⁺ selectivity. This glycine residue is well conserved among subdomains I and III of eukaryotic Cavs. These findings provide new insight into the Ca²⁺ selectivity mechanism that is conserved from prokaryotes to eukaryotes.

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