7YO0: PDB entry 7YO0

Cryo-EM structure of human Slo1-LRRC26 complex with Symmetry Expansion. Determined by electron microscopy at 3.6 Å resolution. Released 6 Mar 2024.

Method: Electron microscopy
Resolution: 3.6 Å
Organism: Homo sapiens
Chains: 8
Atoms: 36,004
Mol. weight: 620.82 kDa
Ligands: CA, MG, PGW
Released: 6 Mar 2024

Explore 7YO0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7YO0 contains 220 α-helices and 160 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.

Chains A, C, E and G: 45 helices, 28 β-strands

Element	Residues	Length	Sheet
α-helix	23-48	26
α-helix	93-105	13
α-helix	110-133	24
β-strand	139-140	2	1
α-helix	144-146	3
α-helix	149-170	22
α-helix	174-178	5
α-helix	181-199	19
β-strand	202-203	2	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	385-392	8
β-strand	398-402	5	2
α-helix	408-413	6
α-helix	416-418	3
β-strand	419-425	7	2
α-helix	433-450	18
β-strand	456-460	5	2
α-helix	463-470	8
β-strand	482-485	4	2
α-helix	486-499	14
α-helix	503-509	7
α-helix	524-528	5
β-strand	537-540	4	3
α-helix	550-554	5
α-helix	558-561	4
β-strand	565	1	3
β-strand	594-597	4	3
β-strand	686	1	4
β-strand	692	1	5
β-strand	693	1	4
α-helix	700-702	3
β-strand	704	1	6
α-helix	707-712	6
β-strand	719-724	6	6
α-helix	735-738	4
β-strand	743	1	5
α-helix	751-753	3
β-strand	754-758	5	6
α-helix	760-765	6
α-helix	766-768	3
β-strand	776-779	4	6
α-helix	786-791	6
β-strand	799-804	6	6
α-helix	806-808	3
α-helix	818-829	12
β-strand	831	1	7
β-strand	872	1	7
α-helix	873-875	3
β-strand	878-881	4	6
α-helix	885-890	6
α-helix	903-905	3
α-helix	907-910	4
β-strand	914-915	2	6
α-helix	917-920	4
α-helix	923-929	7
α-helix	932-940	9
α-helix	947-956	10
α-helix	966-970	5
β-strand	976-980	5	8
α-helix	986-990	5
α-helix	996-1007	12
β-strand	1013-1017	5	8
β-strand	1031-1035	5	8
β-strand	1048-1053	6	8

Chains B, D, F and H: 10 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	48-50	3	9
β-strand	54-56	3	9
β-strand	75-77	3	9
β-strand	85-86	2	10
β-strand	99-101	3	9
β-strand	109-110	2	10
β-strand	123-125	3	9
β-strand	147-149	3	9
α-helix	160-163	4
β-strand	171-173	3	9
α-helix	182-183	2
α-helix	187-189	3
β-strand	195-197	3	9
β-strand	204	1	11
α-helix	207-209	3
α-helix	210-218	9
α-helix	223-226	4
β-strand	233	1	11
α-helix	235-237	3
α-helix	242-244	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, C, E, G	protein	1060	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

>7YO0_1 Calcium-activated potassium channel subunit alpha-1 (chains A, C, E, G)
MDALIIPVTMEVPCDSRGQRMWWAFLASSMVTFFGGLFIILLWRTLKYLWTVCCHCGGKT
KEAQKINNGSSQADGTLKPVDEKEEAVAAEVGWMTSVKDWAGVMISAQTLTGRVLVVLVF
ALSIGALVIYFIDSSNPIESCQNFYKDFTLQIDMAFNVFFLLYFGLRFIAANDKLWFWLE
VNSVVDFFTVPPVFVSVYLNRSWLGLRFLRALRLIQFSEILQFLNILKTSNSIKLVNLLS
IFISTWLTAAGFIHLVENSGDPWENFQNNQALTYWECVYLLMVTMSTVGYGDVYAKTTLG
RLFMVFFILGGLAMFASYVPEIIELIGNRKKYGGSYSAVSGRKHIVVCGHITLESVSNFL
KDFLHKDRDDVNVEIVFLHNISPNLELEALFKRHFTQVEFYQGSVLNPHDLARVKIESAD
ACLILANKYCADPDAEDASNIMRVISIKNYHPKIRIITQMLQYHNKAHLLNIPSWNWKEG
DDAICLAELKLGFIAQSCLAQGLSTMLANLFSMRSFIKIEEDTWQKYYLEGVSNEMYTEY
LSSAFVGLSFPTVCELCFVKLKLLMIAIEYKSANRESRSRSRILINPGNHLKIQEGTLGF
FIASDAKEVKRAFFYCKACHDDITDPKRIKKCGCKRLEDEQPSTLSPKKKQRNGGMRNSP
NTSPKLMRHDPLLIPGNDQIDNMDSNVKKYDSTGMFHWCAPKEIEKVILTRSEAAMTVLS
GHVVVCIFGDVSSALIGLRNLVMPLRASNFHYHELKHIVFVGSIEYLKREWETLHNFPKV
SILPGTPLSRADLRAVNINLCDMCVILSANQNNIDDTSLQDKECILASLNIKSMQFDDSI
GVLQANSQGFTPPGMDRSSPDNSPVHGMLRQPSITTGVNIPIITELVNDTNVQFLDQDDD
DDPDTELYLTQPFACGTAFAVSVLDSLMSATYFNDNILTLIRTLVTGGATPELEALIAEE
NALRGGYSTPQTLANRDRCRVAQLALLDGPFADLGDGGCYGDLFCKALKTYNMLCFGIYR
LRDAHLSTPSQCTKRYVITNPPYEFELVPTDLIFCLMQFD

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

>7YO0_2 Leucine-rich repeat-containing protein 26 (chains B, D, F, H)
MRGPSWSRPRPLLLLLLLLSPWPVWAQVSATASPSGSLGAPDCPEVCTCVPGGLASCSAL
SLPAVPPGLSLRLRALLLDHNRVRALPPGAFAGAGALQRLDLRENGLHSVHVRAFWGLGA
LQLLDLSANQLEALAPGTFAPLRALRNLSLAGNRLARLEPAALGALPLLRSLSLQDNELA
ALAPGLLGRLPALDALHLRGNPWGCGCALRPLCAWLRRHPLPASEAETVLCVWPGRLTLS
PLTAFSDAAFSHCAQPLALRDLAVVYTLGPASFLVSLASCLALGSGLTACRARRRRLRTA
ALRPPRPPDPNPDPDPHGCASPADPGSPAAAAQA

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	8
MG	Magnesium ion	Mg	4
PGW	(1R)-2-{[(S)-{[(2S)-2,3-dihydroxypropyl]oxy}(hydroxy)phosphoryl]oxy}-1-[(hexade…	C40 H77 O10 P	4

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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