1.A.2.2.2 The KirBac3.1 K+ channel (a dimer of dimers with gating visualized by atomic force microscopy (Jaroslawski et al., 2007) (regulated by binding lipids, G-proteins, nucleotides, and ions (H+, Ca2+, and Mg2+)). The 3-D structure is available (1XL6_A). The inhibitory cholesterol binding site has been identified (Fürst et al. 2014). The constricted opening in this, and presumably other, Kir channels does not impede potassium conduction (Black et al. 2020). The structural and dynamic properties of a KirBac3.1 mutant revealed the function of a highly conserved tryptophan in the transmembrane domain (Fagnen et al. 2021).
|
Accession Number: | D9N164 |
Protein Name: | Potassium channel |
Length: | 301 |
Molecular Weight: | 33738.00 |
Species: | Magnetospirillum magnetotacticum [188] |
Number of TMSs: | 3 |
Substrate |
potassium(1+) |
---|
1: MTGGMKPPAR KPRILNSDGS SNITRLGLEK RGWLDDHYHD LLTVSWPVFI TLITGLYLVT
61: NALFALAYLA CGDVIENARP GSFTDAFFFS VQTMATIGYG KLIPIGPLAN TLVTLEALCG
121: MLGLAVAASL IYARFTRPTA GVLFSSRMVI SDFEGKPTLM MRLANLRIEQ IIEADVHLVL
181: VRSEISQEGM VFRRFHDLTL TRSRSPIFSL SWTVMHPIDH HSPIYGETDE TLRNSHSEFL
241: VLFTGHHEAF AQNVHARHAY SCDEIIWGGH FVDVFTTLPD GRRALDLGKF HEIAQHHHHH
301: H