4msw

Y78 ester mutant of KcsA in high K+Y78 ester mutant of KcsA in high K+

FunctionFunction

[KCSA_STRLI] Acts as a pH-gated potassium ion channel; changing the cytosolic pH from 7 to 4 opens the channel, although it is not clear if this is the physiological stimulus for channel opening. Monovalent cation preference is K(+) > Rb(+) > NH4(+) >> Na(+) > Li(+).^[1]

About this StructureAbout this Structure

4msw is a 3 chain structure with sequence from Mus musculus and Streptomyces lividans. Full crystallographic information is available from OCA.

ReferenceReference

^{[xtra 1]}

↑ Matulef K, Komarov AG, Costantino CA, Valiyaveetil FI. Using protein backbone mutagenesis to dissect the link between ion occupancy and C-type inactivation in K+ channels. Proc Natl Acad Sci U S A. 2013 Oct 15. PMID:24128761 doi:http://dx.doi.org/10.1073/pnas.1314356110

↑ Schrempf H, Schmidt O, Kummerlen R, Hinnah S, Muller D, Betzler M, Steinkamp T, Wagner R. A prokaryotic potassium ion channel with two predicted transmembrane segments from Streptomyces lividans. EMBO J. 1995 Nov 1;14(21):5170-8. PMID:7489706

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OCA

[2] Matulef K, Komarov AG, Costantino CA, Valiyaveetil FI. Using protein backbone mutagenesis to dissect the link between ion occupancy and C-type inactivation in K+ channels. Proc Natl Acad Sci U S A. 2013 Oct 15. PMID:24128761 doi:http://dx.doi.org/10.1073/pnas.1314356110

[1] Schrempf H, Schmidt O, Kummerlen R, Hinnah S, Muller D, Betzler M, Steinkamp T, Wagner R. A prokaryotic potassium ion channel with two predicted transmembrane segments from Streptomyces lividans. EMBO J. 1995 Nov 1;14(21):5170-8. PMID:7489706

[1]

[xtra 1]