7YO4: RCK1-RCK2 mutated human Slo1-LRRC26 complex

Cryo-EM structure of RCK1-RCK2 mutated human Slo1-LRRC26 complex. Determined by electron microscopy at 3.9 Å resolution. Released 6 Mar 2024.

Method: Electron microscopy
Resolution: 3.9 Å
Organism: Homo sapiens
Chains: 8
Atoms: 35,560
Mol. weight: 615.08 kDa
Released: 6 Mar 2024

Explore 7YO4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7YO4 contains 238 α-helices and 184 β-strands across 8 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 51 helices, 34 β-strands

Element	Residues	Length	Sheet
α-helix	22-33	12
α-helix	95-105	11
α-helix	110-134	25
β-strand	139-140	2	1
α-helix	148-170	23
α-helix	175-178	4
α-helix	181-196	16
β-strand	202-203	2	1
α-helix	207-214	8
α-helix	217-223	7
α-helix	230-258	29
α-helix	262-264	3
α-helix	274-285	12
α-helix	298-317	20
α-helix	320-327	8
β-strand	344-349	6	2
α-helix	353-363	11
β-strand	374-379	6	2
α-helix	382-383	2
α-helix	385-393	9
β-strand	398-402	5	2
α-helix	408-413	6
α-helix	416-418	3
β-strand	421-425	5	2
α-helix	433-450	18
β-strand	455-460	6	2
α-helix	463-471	9
β-strand	482-485	4	2
α-helix	486-499	14
α-helix	503-511	9
α-helix	524-532	9
β-strand	535-540	6	3
α-helix	541-542	2
α-helix	543-545	3
β-strand	549	1	4
α-helix	550-561	12
β-strand	564-570	7	3
β-strand	578-581	4	3
β-strand	588	1	4
β-strand	594-599	6	3
α-helix	602-605	4
α-helix	606-610	5
α-helix	622-625	4
β-strand	686-687	2	5
β-strand	692	1	6
β-strand	693	1	5
α-helix	700-703	4
β-strand	704	1	7
α-helix	707-712	6
β-strand	719-723	5	7
α-helix	730-731	2
α-helix	735-738	4
α-helix	740-742	3
β-strand	743	1	6
α-helix	751-753	3
β-strand	754-758	5	7
α-helix	760-766	7
α-helix	767-769	3
β-strand	776-780	5	7
α-helix	786-792	7
α-helix	794-796	3
β-strand	799-803	5	7
α-helix	815-817	3
α-helix	818-828	11
β-strand	831	1	8
β-strand	872	1	8
β-strand	878-882	5	7
α-helix	885-888	4
α-helix	907-910	4
β-strand	914-916	3	7
α-helix	918-929	12
α-helix	931-938	8
α-helix	939-943	5
α-helix	947-956	10
β-strand	961-962	2	5
α-helix	966-972	7
β-strand	975-981	7	9
α-helix	988-991	4
β-strand	995	1	10
α-helix	996-1007	12
β-strand	1010-1017	8	9
β-strand	1031-1035	5	9
β-strand	1042	1	10
β-strand	1047-1054	8	9
α-helix	1055	1

Chain B: 7 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	79	1	11
α-helix	86-87	2
β-strand	99-100	2	12
β-strand	103	1	11
β-strand	109	1	13
β-strand	123-125	3	12
β-strand	127	1	11
β-strand	133	1	13
α-helix	134-135	2
β-strand	147-149	3	12
α-helix	160-163	4
β-strand	171-173	3	12
α-helix	184-189	6
β-strand	195-197	3	12
β-strand	204	1	14
α-helix	209-218	10
α-helix	221-223	3
β-strand	230-231	2	15
β-strand	232	1	14
β-strand	240-241	2	15
α-helix	259-283	25

Chain C: 51 helices, 34 β-strands

Element	Residues	Length	Sheet
α-helix	22-33	12
α-helix	95-105	11
α-helix	110-134	25
β-strand	139-140	2	16
α-helix	148-170	23
α-helix	181-198	18
β-strand	202-203	2	16
α-helix	207-211	5
α-helix	214-216	3
α-helix	217-223	7
α-helix	230-258	29
α-helix	262-264	3
α-helix	274-285	12
α-helix	298-317	20
α-helix	320-327	8
β-strand	344-349	6	17
α-helix	353-363	11
β-strand	374-379	6	17
α-helix	382-383	2
α-helix	385-393	9
β-strand	398-402	5	17
α-helix	408-413	6
α-helix	416-418	3
β-strand	421-425	5	17
α-helix	433-450	18
β-strand	455-460	6	17
α-helix	463-465	3
α-helix	467-470	4
β-strand	482-485	4	17
α-helix	486-499	14
α-helix	503-511	9
α-helix	524-532	9
β-strand	535-540	6	18
α-helix	541-542	2
α-helix	543-545	3
β-strand	549	1	19
α-helix	550-561	12
β-strand	564-570	7	18
β-strand	578-581	4	18
β-strand	588	1	19
β-strand	594-599	6	18
α-helix	602-605	4
α-helix	606-609	4
α-helix	622-625	4
β-strand	686-687	2	20
β-strand	692	1	21
β-strand	693	1	20
α-helix	700-703	4
β-strand	704	1	22
α-helix	707-712	6
β-strand	719-723	5	22
α-helix	730-731	2
α-helix	735-741	7
β-strand	743	1	21
α-helix	748-750	3
α-helix	751-753	3
β-strand	754-758	5	22
α-helix	760-766	7
α-helix	767-769	3
β-strand	776-780	5	22
α-helix	786-792	7
β-strand	799-803	5	22
α-helix	814-817	4
α-helix	818-828	11
β-strand	831	1	23
β-strand	872	1	23
α-helix	873-875	3
β-strand	878-882	5	22
α-helix	886-890	5
α-helix	907-911	5
β-strand	914-916	3	22
α-helix	918-929	12
α-helix	931-941	11
α-helix	947-956	10
β-strand	961-962	2	20
α-helix	966-971	6
β-strand	975-981	7	24
α-helix	988-991	4
β-strand	995	1	25
α-helix	996-1006	11
β-strand	1011-1017	7	24
β-strand	1031-1035	5	24
β-strand	1042	1	25
β-strand	1047-1054	8	24
α-helix	1055	1

Chain D: 10 helices, 12 β-strands

Element	Residues	Length	Sheet
α-helix	55-57	3
β-strand	85	1	26
α-helix	86-87	2
β-strand	99	1	27
β-strand	102-103	2	28
β-strand	109	1	26
β-strand	123-125	3	27
β-strand	126-127	2	28
α-helix	134-135	2
β-strand	147-149	3	27
α-helix	160-163	4
β-strand	171-173	3	27
α-helix	184-189	6
β-strand	195-197	3	27
β-strand	203-204	2	29
α-helix	207-209	3
α-helix	210-218	9
α-helix	221-223	3
β-strand	230-232	3	29
β-strand	240-241	2	29
α-helix	242-244	3
α-helix	259-283	25

Chain E: 50 helices, 35 β-strands

Element	Residues	Length	Sheet
α-helix	22-33	12
α-helix	95-105	11
α-helix	110-134	25
β-strand	139-140	2	30
α-helix	148-170	23
α-helix	181-196	16
β-strand	202-203	2	30
α-helix	207-216	10
α-helix	217-223	7
α-helix	230-258	29
α-helix	262-264	3
α-helix	274-285	12
α-helix	298-317	20
α-helix	319-327	9
β-strand	344-349	6	31
α-helix	353-363	11
β-strand	374-379	6	31
α-helix	382-383	2
α-helix	385-393	9
β-strand	398-402	5	31
α-helix	408-413	6
β-strand	421-425	5	31
α-helix	433-450	18
β-strand	455-460	6	31
α-helix	463-471	9
β-strand	482-485	4	31
α-helix	486-499	14
α-helix	503-511	9
α-helix	524-532	9
β-strand	535-540	6	32
α-helix	541-542	2
α-helix	543-545	3
β-strand	549	1	33
α-helix	550-556	7
α-helix	557-561	5
β-strand	564-570	7	32
β-strand	578-581	4	32
β-strand	588	1	33
β-strand	594-599	6	32
α-helix	602-605	4
α-helix	606-608	3
α-helix	622-625	4
β-strand	686-687	2	34
β-strand	692	1	35
β-strand	693	1	34
β-strand	704	1	36
α-helix	707-712	6
β-strand	719-723	5	36
α-helix	730-731	2
α-helix	735-741	7
β-strand	743	1	35
α-helix	751-753	3
β-strand	754-758	5	36
α-helix	760-766	7
α-helix	767-769	3
β-strand	776-780	5	36
α-helix	786-791	6
α-helix	794-796	3
β-strand	799-803	5	36
α-helix	814-817	4
α-helix	818-828	11
β-strand	831	1	37
β-strand	872	1	37
β-strand	878-882	5	36
α-helix	886-890	5
α-helix	907-911	5
β-strand	914-916	3	36
α-helix	918-929	12
α-helix	932-938	7
α-helix	939-943	5
α-helix	947-956	10
β-strand	961-962	2	34
α-helix	966-971	6
β-strand	975-981	7	38
α-helix	988-991	4
β-strand	995	1	39
α-helix	996-1006	11
α-helix	1009	1
β-strand	1010	1	38
α-helix	1011	1
β-strand	1013-1017	5	38
β-strand	1031-1035	5	38
β-strand	1042	1	39
β-strand	1048-1054	7	38
α-helix	1055	1

Chain F: 9 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	86-87	2
β-strand	99-100	2	40
β-strand	103	1	41
β-strand	123-125	3	40
β-strand	127	1	41
α-helix	134-135	2
β-strand	147-149	3	40
α-helix	160-163	4
β-strand	171-173	3	40
α-helix	184-189	6
β-strand	195-197	3	40
β-strand	203-204	2	42
α-helix	207-209	3
α-helix	210-218	9
α-helix	221-223	3
β-strand	230-232	3	42
β-strand	240-241	2	42
α-helix	242-244	3
α-helix	259-282	24

Chain G: 52 helices, 36 β-strands

Element	Residues	Length	Sheet
α-helix	22-33	12
α-helix	95-105	11
α-helix	110-134	25
β-strand	139-140	2	43
α-helix	148-170	23
α-helix	175-178	4
α-helix	181-198	18
β-strand	202-203	2	43
α-helix	207-211	5
α-helix	217-223	7
α-helix	230-258	29
α-helix	274-285	12
α-helix	298-317	20
α-helix	319-327	9
β-strand	339	1	44
β-strand	342	1	44
β-strand	344-349	6	45
α-helix	353-363	11
β-strand	374-379	6	45
α-helix	382-384	3
α-helix	385-393	9
β-strand	398-402	5	45
α-helix	408-413	6
β-strand	421-425	5	45
α-helix	433-450	18
β-strand	455-460	6	45
α-helix	463-466	4
α-helix	467-470	4
β-strand	482-485	4	45
α-helix	486-499	14
α-helix	503-511	9
α-helix	524-532	9
β-strand	535-540	6	46
α-helix	541-542	2
α-helix	543-545	3
β-strand	549	1	47
α-helix	550-559	10
β-strand	564-570	7	46
β-strand	578-581	4	46
β-strand	588	1	47
β-strand	594-599	6	46
α-helix	602-605	4
α-helix	606-608	3
α-helix	622-625	4
β-strand	686-687	2	48
β-strand	692	1	49
β-strand	693	1	48
α-helix	700-703	4
β-strand	704	1	50
α-helix	707-712	6
β-strand	719-723	5	50
α-helix	730-731	2
α-helix	735-738	4
α-helix	739-741	3
β-strand	743	1	49
α-helix	748-750	3
α-helix	751-753	3
β-strand	754-758	5	50
α-helix	760-766	7
α-helix	767-769	3
β-strand	776-780	5	50
α-helix	786-792	7
β-strand	799-803	5	50
α-helix	814-817	4
α-helix	818-828	11
β-strand	831	1	51
β-strand	872	1	51
α-helix	873-875	3
β-strand	878-882	5	50
α-helix	886-890	5
α-helix	907-910	4
β-strand	914-916	3	50
α-helix	918-929	12
α-helix	932-938	7
α-helix	939-943	5
α-helix	947-956	10
β-strand	961-962	2	48
α-helix	966-972	7
β-strand	975-981	7	52
α-helix	989-991	3
β-strand	995	1	53
α-helix	996-1002	7
α-helix	1003-1007	5
β-strand	1010-1017	8	52
β-strand	1031-1035	5	52
β-strand	1042	1	53
β-strand	1047-1054	8	52
α-helix	1055	1

Chain H: 8 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	85	1	54
α-helix	86-87	2
β-strand	99	1	55
β-strand	109	1	54
β-strand	123-125	3	55
α-helix	134-135	2
β-strand	147-149	3	55
α-helix	160-163	4
β-strand	171-173	3	55
α-helix	184-189	6
β-strand	195-197	3	55
α-helix	207-209	3
α-helix	210-218	9
α-helix	221-223	3
β-strand	230	1	56
β-strand	241	1	56
α-helix	259-283	25

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Calcium-activated potassium channel subunit alpha-1	A, C, E, G	protein	1056	Homo sapiens	Q12791 (AlphaFold model)
Leucine-rich repeat-containing protein 26	B, D, F, H	protein	334	Homo sapiens	Q2I0M4 (AlphaFold model)

Sequence of entity 1 (A, C, E, G), FASTA

>7YO4_1 Calcium-activated potassium channel subunit alpha-1 (chains A, C, E, G)
MDALIIPVTMEVPCDSRGQRMWWAFLASSMVTFFGGLFIILLWRTLKYLWTVCCHCGGKT
KEAQKINNGSSQADGTLKPVDEKEEAVAAEVGWMTSVKDWAGVMISAQTLTGRVLVVLVF
ALSIGALVIYFIDSSNPIESCQNFYKDFTLQIDMAFNVFFLLYFGLRFIAANDKLWFWLE
VNSVVDFFTVPPVFVSVYLNRSWLGLRFLRALRLIQFSEILQFLNILKTSNSIKLVNLLS
IFISTWLTAAGFIHLVENSGDPWENFQNNQALTYWECVYLLMVTMSTVGYGDVYAKTTLG
RLFMVFFILGGLAMFASYVPEIIELIGNRKKYGGSYSAVSGRKHIVVCGHITLESVSNFL
KAFLHKARDDVNVEIVFLHNISPNLELEALFKRHFTQVEFYQGSVLNPHDLARVKIESAD
ACLILANKYCADPDAEDASNIMRVISIKNYHPKIRIITQMLQYHNKAHLLNIPSWNWKEG
DDAICLAELKLGFIAQSCLAQGLSTMLANLFSMRSFIKIEEDTWQKYYLEGVSNEMYTEY
LSSAFVGLSFPTVCELCFVKLKLLMIAIEYKSANRESRILINPGNHLKIQEGTLGFFIAS
DAKEVKRAFFYCKACHDDITDPKRIKKCGCKRLEDEQPSTLSPKKKQRNGGMRNSPNTSP
KLMRHDPLLIPGNDQIDNMDSNVKKYDSTGMFHWCAPKEIEKVILTRSEAAMTVLSGHVV
VCIFGDVSSALIGLRNLVMPLRASNFHYHELKHIVFVGSIEYLKREWETLHNFPKVSILP
GTPLSRADLRAVNINLCDMCVILSANQNNIDDTSLQDKECILASLNIKSMQFDDSIGVLQ
ANSQGFTPPGMDRSSPDNSPVHGMLRQPSITTGVNIPIITELVNDTNVQFLDQNNNNNPD
TELYLTQPFACGTAFAVSVLDSLMSATYFNDNILTLIRTLVTGGATPELEALIAEENALR
GGYSTPQTLANRDRCRVAQLALLDGPFADLGDGGCYGDLFCKALKTYNMLCFGIYRLRDA
HLSTPSQCTKRYVITNPPYEFELVPTDLIFCLMQFD

Sequence of entity 2 (B, D, F, H), FASTA

>7YO4_2 Leucine-rich repeat-containing protein 26 (chains B, D, F, H)
MRGPSWSRPRPLLLLLLLLSPWPVWAQVSATASPSGSLGAPDCPEVCTCVPGGLASCSAL
SLPAVPPGLSLRLRALLLDHNRVRALPPGAFAGAGALQRLDLRENGLHSVHVRAFWGLGA
LQLLDLSANQLEALAPGTFAPLRALRNLSLAGNRLARLEPAALGALPLLRSLSLQDNELA
ALAPGLLGRLPALDALHLRGNPWGCGCALRPLCAWLRRHPLPASEAETVLCVWPGRLTLS
PLTAFSDAAFSHCAQPLALRDLAVVYTLGPASFLVSLASCLALGSGLTACRARRRRLRTA
ALRPPRPPDPNPDPDPHGCASPADPGSPAAAAQA

Primary citation

Structural basis for dual allosteric gating modulation of Slo1-LRRC channel complex. Yamanouchi, D. To be published.

Other PDB entries of the same protein (UniProt Q12791 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6V5A 2.0 Å, Crystal structure of the human BK channel gating ring L390P mutant
8V60 2.43 Å, F315A mutant of human Slo1 in presence of EDTA - resting VSD
11DA 2.57 Å, Human Slo1-PenitremA complex under divalent chelated condition - full model
9CZM 2.57 Å, Ca2+ bound open-inactivated hSlo1 + beta2N-beta4 channel in nanodisc.
11DC 2.58 Å, Human Slo1-PenitremA complex under divalent chelated condition - gating-ring masked out
11CZ 2.6 Å, Human Slo1-paxilline complex under divalent chelated condition - full model
8V64 2.6 Å, RCK1-RCK2 double mutant of human Slo1 in presence of EDTA - resting VSD
8GHF 2.7 Å, cryo-EM structure of hSlo1 in plasma membrane vesicles
11DB 2.71 Å, Human Slo1-Paxilline complex under divalent chelated condition - gating-ring masked
8V63 2.72 Å, R207A mutant of human Slo1 in presence of EDTA - activated VSD
9JO3 2.8 Å, Cryo-EM structure of human BKca channel-compound 10b complex
8VAZ 2.82 Å, Structure of human Slo1 and human LRRC26 in EDTA - LRRD masked

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