7YO3: Human Slo1-LRRC26 complex with C4 symmetry

Cryo-EM structure of human Slo1-LRRC26 complex with C4 symmetry. Determined by electron microscopy at 3.1 Å resolution. Released 30 Aug 2023.

Method: Electron microscopy
Resolution: 3.1 Å
Organism: Homo sapiens
Chains: 2
Atoms: 8,961
Mol. weight: 154.46 kDa
Ligands: CA, MG
Released: 30 Aug 2023

Explore 7YO3 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7YO3 contains 57 α-helices and 41 β-strands across 2 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: 47 helices, 29 β-strands

Element	Residues	Length	Sheet
α-helix	22-48	27
α-helix	93-105	13
α-helix	110-133	24
β-strand	139-141	3	1
α-helix	149-170	22
α-helix	174-178	5
α-helix	181-187	7
α-helix	190-199	10
β-strand	201-203	3	1
α-helix	206-214	9
α-helix	218-223	6
α-helix	230-258	29
α-helix	262-264	3
α-helix	274-285	12
α-helix	298-326	29
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
β-strand	422-425	4	2
α-helix	433-450	18
β-strand	456-458	3	2
β-strand	459-460	2	3
α-helix	463-470	8
β-strand	484-485	2	3
α-helix	486-499	14
α-helix	503-509	7
α-helix	524-532	9
β-strand	537-540	4	4
α-helix	541-542	2
α-helix	550-554	5
α-helix	558-561	4
β-strand	565	1	4
β-strand	594-597	4	4
β-strand	686	1	5
β-strand	692	1	6
β-strand	693	1	5
α-helix	700-702	3
β-strand	704	1	7
α-helix	707-712	6
β-strand	719-724	6	7
α-helix	735-738	4
α-helix	739-742	4
β-strand	743	1	6
α-helix	751-753	3
β-strand	754-758	5	7
α-helix	760-765	6
β-strand	776-779	4	7
α-helix	786-791	6
α-helix	794-796	3
β-strand	799-804	6	7
α-helix	806-808	3
α-helix	818-829	12
β-strand	831	1	8
β-strand	872	1	8
α-helix	873-875	3
β-strand	878-881	4	7
α-helix	885-887	3
α-helix	888-891	4
α-helix	903-905	3
α-helix	907-910	4
β-strand	914-915	2	7
α-helix	917-919	3
α-helix	923-929	7
α-helix	932-940	9
α-helix	947-955	9
α-helix	966-970	5
β-strand	976-980	5	9
α-helix	986-988	3
α-helix	996-1007	12
β-strand	1013-1017	5	9
β-strand	1031-1035	5	9
β-strand	1047-1053	7	9

Chain B: 10 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	48-50	3	10
β-strand	54-56	3	10
β-strand	75-77	3	10
β-strand	85-86	2	11
β-strand	99-101	3	10
β-strand	109-110	2	11
β-strand	123-125	3	10
β-strand	147-149	3	10
α-helix	160-163	4
β-strand	171-173	3	10
α-helix	182-183	2
α-helix	187-189	3
β-strand	195-197	3	10
α-helix	207-209	3
α-helix	210-218	9
α-helix	223-226	4
β-strand	230	1	12
β-strand	241	1	12
α-helix	242-244	3
α-helix	248-250	3
α-helix	255-257	3
α-helix	260-296	37

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Calcium-activated potassium channel subunit alpha-1	A	protein	1060	Homo sapiens	Q12791 (AlphaFold model)
Leucine-rich repeat-containing protein 26	B	protein	334	Homo sapiens	Q2I0M4 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>7YO3_1 Calcium-activated potassium channel subunit alpha-1 (chains A)
MDALIIPVTMEVPCDSRGQRMWWAFLASSMVTFFGGLFIILLWRTLKYLWTVCCHCGGKT
KEAQKINNGSSQADGTLKPVDEKEEAVAAEVGWMTSVKDWAGVMISAQTLTGRVLVVLVF
ALSIGALVIYFIDSSNPIESCQNFYKDFTLQIDMAFNVFFLLYFGLRFIAANDKLWFWLE
VNSVVDFFTVPPVFVSVYLNRSWLGLRFLRALRLIQFSEILQFLNILKTSNSIKLVNLLS
IFISTWLTAAGFIHLVENSGDPWENFQNNQALTYWECVYLLMVTMSTVGYGDVYAKTTLG
RLFMVFFILGGLAMFASYVPEIIELIGNRKKYGGSYSAVSGRKHIVVCGHITLESVSNFL
KDFLHKDRDDVNVEIVFLHNISPNLELEALFKRHFTQVEFYQGSVLNPHDLARVKIESAD
ACLILANKYCADPDAEDASNIMRVISIKNYHPKIRIITQMLQYHNKAHLLNIPSWNWKEG
DDAICLAELKLGFIAQSCLAQGLSTMLANLFSMRSFIKIEEDTWQKYYLEGVSNEMYTEY
LSSAFVGLSFPTVCELCFVKLKLLMIAIEYKSANRESRSRSRILINPGNHLKIQEGTLGF
FIASDAKEVKRAFFYCKACHDDITDPKRIKKCGCKRLEDEQPSTLSPKKKQRNGGMRNSP
NTSPKLMRHDPLLIPGNDQIDNMDSNVKKYDSTGMFHWCAPKEIEKVILTRSEAAMTVLS
GHVVVCIFGDVSSALIGLRNLVMPLRASNFHYHELKHIVFVGSIEYLKREWETLHNFPKV
SILPGTPLSRADLRAVNINLCDMCVILSANQNNIDDTSLQDKECILASLNIKSMQFDDSI
GVLQANSQGFTPPGMDRSSPDNSPVHGMLRQPSITTGVNIPIITELVNDTNVQFLDQDDD
DDPDTELYLTQPFACGTAFAVSVLDSLMSATYFNDNILTLIRTLVTGGATPELEALIAEE
NALRGGYSTPQTLANRDRCRVAQLALLDGPFADLGDGGCYGDLFCKALKTYNMLCFGIYR
LRDAHLSTPSQCTKRYVITNPPYEFELVPTDLIFCLMQFD

Sequence of entity 2 (B), FASTA

>7YO3_2 Leucine-rich repeat-containing protein 26 (chains B)
MRGPSWSRPRPLLLLLLLLSPWPVWAQVSATASPSGSLGAPDCPEVCTCVPGGLASCSAL
SLPAVPPGLSLRLRALLLDHNRVRALPPGAFAGAGALQRLDLRENGLHSVHVRAFWGLGA
LQLLDLSANQLEALAPGTFAPLRALRNLSLAGNRLARLEPAALGALPLLRSLSLQDNELA
ALAPGLLGRLPALDALHLRGNPWGCGCALRPLCAWLRRHPLPASEAETVLCVWPGRLTLS
PLTAFSDAAFSHCAQPLALRDLAVVYTLGPASFLVSLASCLALGSGLTACRARRRRLRTA
ALRPPRPPDPNPDPDPHGCASPADPGSPAAAAQA

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	2
MG	Magnesium ion	Mg	1

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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