Crystal structure of a Kir3.1-prokaryotic Kir channel chimera.
The Kir3.1 K(+) channel participates in heart rate control and neuronal excitability through G-protein and lipid signaling pathways. Expression in Escherichia coli has been achieved by replacing three fourths of the transmembrane pore with the pore of a prokaryotic Kir channel, leaving the cytoplasmic pore and membrane interfacial regions of Kir3.1 origin. Two structures were determined at 2.2 A. The selectivity filter is identical to the Streptomyces lividans K(+) channel within error of measurement (r.m.s.d.<0.2 A), suggesting that K(+) selectivity requires extreme conservation of three-dimensional structure. Multiple K(+) ions reside within the pore and help to explain voltage-dependent Mg(2+) and polyamine blockade and strong rectification. Two constrictions, at the inner helix bundle and at the apex of the cytoplasmic pore, may function as gates: in one structure the apex is open and in the other, it is closed. Gating of the apex is mediated by rigid-body movements of the cytoplasmic pore subunits. Phosphatidylinositol 4,5-biphosphate-interacting residues suggest a possible mechanism by which the signaling lipid regulates the cytoplasmic pore.
Nishida
Motohiko
M
Laboratory of Molecular Neurobiology and Biophysics, Howard Hughes Medical Institute, Rockefeller University, New York, NY 10065, USA.
Cadene
Martine
M
Chait
Brian T
BT
MacKinnon
Roderick
R
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics*; D001665:Binding Sites; D019117:Burkholderia / Q000378:metabolism; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000378:metabolism; D051676:G Protein-Coupled Inwardly-Rectifying Potassium Channels / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics; D015640:Ion Channel Gating; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics
D001426:Bacterial Proteins; D051676:G Protein-Coupled Inwardly-Rectifying Potassium Channels; D011993:Recombinant Fusion Proteins
J Biol Chem. 1999 Apr 30;274(18):12517-24
10212228
Proc Natl Acad Sci U S A. 1999 May 11;96(10):5820-5
10318968
Nat Cell Biol. 1999 Jul;1(3):183-8
10559906
J Gen Physiol. 2000 Nov;116(5):599-608
11055989
Neuron. 2001 Mar;29(3):657-67
11301025
Neuron. 2001 Mar;29(3):669-80
11301026
Mol Pharmacol. 2001 May;59(5):1086-93
11306691
Cell. 2001 May 18;105(4):511-9
11371347
Nature. 2001 Nov 1;414(6859):43-8
11689936
Sci STKE. 2001 Dec 04;2001(111):re19
11734659
BMC Evol Biol. 2001;1:14
11806753
Am J Physiol Renal Physiol. 2002 May;282(5):F826-34
11934692
Neuron. 2002 Jun 13;34(6):933-44
12086641
J Clin Invest. 2002 Aug;110(3):381-8
12163457
Rev Physiol Biochem Pharmacol. 2002;145:47-179
12224528
Cell. 2002 Dec 27;111(7):957-65
12507423
J Biol Chem. 2003 Mar 21;278(12):10500-5
12514171
J Membr Biol. 2003 Mar 15;192(2):111-22
12682799
Science. 2003 Jun 20;300(5627):1922-6
12738871
J Biol Chem. 2003 Aug 1;278(31):29174-83
12743112
Biophys J. 2003 Jun;84(6):3717-29
12770878
J Biol Chem. 2003 Dec 19;278(51):51779-85
14522976
J Gen Physiol. 2003 Nov;122(5):485-500
14581581
J Mol Biol. 2003 Nov 7;333(5):965-75
14583193
J Physiol. 2004 Mar 16;555(Pt 3):643-57
14724209
Annu Rev Physiol. 2004;66:103-29
14977398
J Biol Chem. 2004 Sep 3;279(36):37271-81
15155739
Acta Crystallogr D Biol Crystallogr. 1994 Sep 1;50(Pt 5):760-3
15299374
Physiol Rev. 2005 Jan;85(1):319-71
15618483
EMBO J. 2005 Jan 26;24(2):229-39
15650751
Nat Neurosci. 2005 Mar;8(3):279-87
15723059
J Physiol. 2005 Apr 15;564(Pt 2):489-500
15731196
J Gen Physiol. 2005 Apr;125(4):413-26
15795311
EMBO Rep. 2005 May;6(5):470-5
15864298
Diabetes. 2005 Sep;54(9):2503-13
16123337
J Physiol. 2006 Mar 1;571(Pt 2):303-17
16373383
Biochem Soc Trans. 2006 Apr;34(Pt 2):243-6
16545085
EMBO Rep. 2006 Jun;7(6):611-6
16641935
Biochemistry. 2006 Jul 18;45(28):8599-606
16834334
Biophys J. 2006 Oct 15;91(8):2901-9
16891366
J Biol Chem. 2007 Feb 23;282(8):5781-9
17166852
PLoS Biol. 2007 May;5(5):e121
17472437
Nature. 1987 Jan 22-28;325(6102):321-6
2433589
Nature. 1987 Jan 8-14;325(7000):156-9
2433601
Proc Natl Acad Sci U S A. 1987 Apr;84(8):2560-4
2436236
Methods Enzymol. 1997;276:307-26
27754618
Science. 1995 Apr 21;268(5209):423-6
7716547
Neuron. 1995 May;14(5):1047-54
7748552
Nature. 1995 Mar 9;374(6518):135-41
7877685
Nature. 1994 Nov 24;372(6504):366-9
7969496
Nature. 1994 Jul 14;370(6485):143-6
8022483
Nature. 1994 Mar 17;368(6468):255-7
8145826
Science. 1994 May 6;264(5160):844-7
8171340
Science. 1996 Aug 16;273(5277):956-9
8688080
Nat Genet. 1996 Oct;14(2):152-6
8841184
J Biol Chem. 1997 Feb 28;272(9):5388-95
9038137
Nature. 1998 Feb 19;391(6669):803-6
9486652
Science. 1998 Apr 3;280(5360):69-77
9525859
J Gen Physiol. 1998 Sep;112(3):333-49
9725893
Acta Crystallogr D Biol Crystallogr. 1998 Sep 1;54(Pt 5):905-21
9757107
Science. 1998 Nov 6;282(5391):1138-41
9804554
Science. 1998 Nov 6;282(5391):1141-4
9804555