8F8Q: CapZ-capped barbed end of F-actin

Cryo-EM structure of the CapZ-capped barbed end of F-actin. Determined by electron microscopy at 2.79 Å resolution. Released 7 Jun 2023.

Method: Electron microscopy
Resolution: 2.79 Å
Organisms: Oryctolagus cuniculus, Homo sapiens
Chains: 8
Atoms: 22,006
Mol. weight: 319.59 kDa
Ligands: MG, ADP
Released: 7 Jun 2023

Explore 8F8Q in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8F8Q contains 152 α-helices and 142 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: 22 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	5-7	3
β-strand	8-12	5	1
β-strand	16-21	6	1
β-strand	29-32	4	1
β-strand	35-38	4	2
β-strand	53-54	2	2
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	2
β-strand	71-72	2	3
β-strand	75-76	2	3
α-helix	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	1
α-helix	113-125	13
β-strand	131-136	6	1
α-helix	137-144	8
β-strand	150-155	6	4
β-strand	160-166	7	4
β-strand	169-170	2	4
α-helix	172-174	3
β-strand	176-178	3	4
α-helix	182-192	11
α-helix	193-196	4
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	5
β-strand	247-250	4	5
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-267	4
α-helix	274-283	10
α-helix	290-294	5
β-strand	297-300	4	4
α-helix	309-320	12
β-strand	329-330	2	4
α-helix	338-346	9
β-strand	357-358	2	1
α-helix	359-365	7
α-helix	370-373	4

Chain B: 21 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	5-7	3
β-strand	8-12	5	6
β-strand	16-21	6	6
β-strand	29-32	4	6
β-strand	35-38	4	7
β-strand	53-54	2	7
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	7
β-strand	71-72	2	8
β-strand	75-76	2	8
α-helix	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	6
α-helix	113-125	13
β-strand	131-136	6	6
α-helix	137-145	9
β-strand	150-155	6	9
β-strand	160-166	7	9
β-strand	169-170	2	9
α-helix	172-174	3
β-strand	176-178	3	9
α-helix	182-192	11
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	10
β-strand	247-250	4	10
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-267	4
α-helix	274-283	10
α-helix	290-294	5
β-strand	297-300	4	9
α-helix	309-320	12
β-strand	329-330	2	9
α-helix	338-346	9
β-strand	357-358	2	6
α-helix	359-365	7
α-helix	369-373	5

Chain C: 22 helices, 20 β-strands

Element	Residues	Length	Sheet
α-helix	5-7	3
β-strand	8-12	5	11
β-strand	16-21	6	11
β-strand	29-32	4	11
β-strand	35-38	4	12
β-strand	41-42	2	4
β-strand	53-54	2	12
α-helix	56-60	5
β-strand	65-68	4	12
β-strand	71-72	2	13
β-strand	75-76	2	13
α-helix	79-88	10
α-helix	89-93	5
α-helix	98-100	3
β-strand	103-107	5	11
α-helix	113-125	13
β-strand	131-136	6	11
α-helix	137-145	9
β-strand	150-155	6	14
β-strand	160-166	7	14
β-strand	169-170	2	14
α-helix	172-174	3
β-strand	176-178	3	14
α-helix	182-192	11
α-helix	193-196	4
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	15
β-strand	247-250	4	15
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-267	4
α-helix	274-283	10
α-helix	290-294	5
β-strand	297-300	4	14
α-helix	303-305	3
α-helix	309-320	12
β-strand	329-330	2	14
α-helix	338-346	9
β-strand	357-358	2	11
α-helix	359-365	7
α-helix	369-373	5

Chain D: 23 helices, 20 β-strands

Element	Residues	Length	Sheet
α-helix	5-7	3
β-strand	8-12	5	16
β-strand	16-21	6	16
β-strand	29-32	4	16
β-strand	35-38	4	17
β-strand	41-42	2	9
β-strand	53-54	2	17
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	17
β-strand	71-72	2	18
β-strand	75-76	2	18
α-helix	79-88	10
α-helix	89-93	5
α-helix	98-100	3
β-strand	103-107	5	16
α-helix	113-125	13
β-strand	131-136	6	16
α-helix	137-144	8
β-strand	150-155	6	19
β-strand	160-166	7	19
β-strand	169-170	2	19
α-helix	172-174	3
β-strand	176-178	3	19
α-helix	182-192	11
α-helix	193-195	3
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	20
β-strand	247-250	4	20
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-267	4
α-helix	274-283	10
α-helix	287-289	3
α-helix	290-294	5
β-strand	297-300	4	19
α-helix	309-320	12
β-strand	329-330	2	19
α-helix	338-346	9
β-strand	357-358	2	16
α-helix	359-365	7
α-helix	369-373	5

Chain E: 22 helices, 20 β-strands

Element	Residues	Length	Sheet
α-helix	6-7	2
β-strand	8-12	5	21
β-strand	16-21	6	21
β-strand	29-32	4	21
β-strand	35-38	4	22
β-strand	41-42	2	14
β-strand	53-54	2	22
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	22
β-strand	71-72	2	23
β-strand	75-76	2	23
α-helix	79-88	10
α-helix	89-93	5
β-strand	103-107	5	21
α-helix	113-125	13
β-strand	131-136	6	21
α-helix	137-145	9
β-strand	150-155	6	24
β-strand	160-166	7	24
β-strand	169-170	2	24
α-helix	172-174	3
β-strand	176-178	3	24
α-helix	182-192	11
α-helix	193-195	3
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	25
β-strand	247-250	4	25
α-helix	253-256	4
α-helix	264-267	4
α-helix	274-283	10
α-helix	290-295	6
β-strand	297-300	4	24
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	24
α-helix	335-337	3
α-helix	339-347	9
β-strand	357-358	2	21
α-helix	359-365	7
α-helix	370-373	4

Chain F: 22 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	26
β-strand	16-21	6	26
β-strand	22	1	27
β-strand	24	1	27
β-strand	29-32	4	26
β-strand	35-38	4	28
β-strand	41-42	2	19
β-strand	53-54	2	28
α-helix	56-59	4
α-helix	62-64	3
β-strand	65-68	4	28
β-strand	71-72	2	29
β-strand	75-76	2	29
α-helix	79-88	10
α-helix	89-93	5
β-strand	103-107	5	26
α-helix	113-125	13
β-strand	131-136	6	26
α-helix	137-144	8
β-strand	150-155	6	30
β-strand	160-166	7	30
β-strand	169-170	2	30
α-helix	172-174	3
β-strand	176-178	3	30
α-helix	182-192	11
α-helix	203-216	14
α-helix	223-230	8
β-strand	238-241	4	31
β-strand	247-250	4	31
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-266	3
α-helix	272-273	2
α-helix	274-283	10
α-helix	287-295	9
β-strand	297-300	4	30
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	30
α-helix	339-347	9
α-helix	351-354	4
β-strand	357-358	2	26
α-helix	359-365	7
α-helix	369-371	3

Chain G: 11 helices, 12 β-strands

Element	Residues	Length	Sheet
α-helix	10-22	13
α-helix	24-25	2
α-helix	30-40	11
α-helix	43-47	5
α-helix	52-61	10
β-strand	63-65	3	32
β-strand	74-76	3	32
β-strand	81	1	33
β-strand	86-89	4	33
β-strand	94-99	6	33
β-strand	104-110	7	33
α-helix	119-135	17
β-strand	139-147	9	34
β-strand	152-161	10	34
β-strand	164	1	34
α-helix	165-167	3
β-strand	169-180	12	34
β-strand	185-198	14	34
β-strand	203-217	15	34
α-helix	221-248	28
α-helix	250-254	5
α-helix	274-278	5
α-helix	279-281	3

Chain H: 9 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	3-14	12
α-helix	21-26	6
α-helix	36-39	4
β-strand	48-52	5	35
β-strand	57-61	5	35
β-strand	66-67	2	36
β-strand	70-72	3	36
β-strand	79-80	2	36
α-helix	91-111	21
β-strand	116-123	8	34
β-strand	128-137	10	34
β-strand	145-158	14	34
β-strand	164-181	18	34
β-strand	185-202	18	34
α-helix	209-227	19
α-helix	228-232	5
α-helix	233-243	11
α-helix	252-255	4
α-helix	258-270	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Actin, alpha skeletal muscle	A, B, C, D, E, F	protein	377	Oryctolagus cuniculus	P68135 (AlphaFold model)
F-actin-capping protein subunit alpha-1	G	protein	286	Homo sapiens	P52907 (AlphaFold model)
F-actin-capping protein subunit beta	H	protein	276	Homo sapiens	P47756 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E, F), FASTA

>8F8Q_1 Actin, alpha skeletal muscle (chains A, B, C, D, E, F)
MCDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEA
QSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREK
MTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRL
DLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEK
SYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNV
MSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWIT
KQEYDEAGPSIVHRKCF

Sequence of entity 2 (G), FASTA

>8F8Q_2 F-actin-capping protein subunit alpha-1 (chains G)
MADFDDRVSDEEKVRIAAKFITHAPPGEFNEVFNDVRLLLNNDNLLREGAAHAFAQYNMD
QFTPVKIEGYEDQVLITEHGDLGNSRFLDPRNKISFKFDHLRKEASDPQPEEADGGLKSW
RESCDSALRAYVKDHYSNGFCTVYAKTIDGQQTIIACIESHQFQPKNFWNGRWRSEWKFT
ITPPTAQVVGVLKIQVHYYEDGNVQLVSHKDVQDSLTVSNEAQTAKEFIKIIENAENEYQ
TAISENYQTMSDTTFKALRRQLPVTRTKIDWNKILSYKIGKEMQNA

Sequence of entity 3 (H), FASTA

>8F8Q_3 F-actin-capping protein subunit beta (chains H)
SDQQLDCALDLMRRLPPQQIEKNLSDLIDLVPSLCEDLLSSVDQPLKIARDKVVGKDYLL
CDYNRDGDSYRSPWSNKYDPPLEDGAMPSARLRKLEVEANNAFDQYRDLYFEGGVSSVYL
WDLDHGFAGVILIKKAGDGSKKIKGCWDSIHVVEVQEKSSGRTAHYKLTSTVMLWLQTNK
SGSGTMNLGGSLTRQMEKDETVSDCSPHIANIGRLVEDMENKIRSTLNEIYFGKTKDIVN
GLRSIDAIPDNQKFKQLQRELSQVLTQRQIYIQPDN

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	6
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	6

Primary citation

Structures of the free and capped ends of the actin filament. Carman, P.J., Barrie, K.R., Rebowski, G. et al. Science (2023) 380:1287-1292. DOI 10.1126/science.adg6812 · PubMed

Other PDB entries of the same protein (UniProt P68135 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4B1Y 1.29 Å, Structure of the Phactr1 RPEL-3 bound to G-actin
2FXU 1.35 Å, X-ray Structure of Bistramide A- Actin Complex at 1.35 A resolution.
4K41 1.4 Å, Crystal structure of actin in complex with marine macrolide kabiramide C
1QZ5 1.45 Å, Structure of rabbit actin in complex with kabiramide C
1WUA 1.45 Å, The structure of Aplyronine A-actin complex
2Q0U 1.45 Å, Structure of Pectenotoxin-2 and Latrunculin B Bound to Actin
2V52 1.45 Å, Structure of MAL-RPEL2 complexed to G-actin
3MN5 1.5 Å, Structures of actin-bound WH2 domains of Spire and the implication for filament nucleation
2PBD 1.5 Å, Ternary complex of profilin-actin with the poly-PRO-GAB domain of VASP*
5ZZA 1.53 Å, OdinProfilin/Rabbit Actin Complex
1J6Z 1.54 Å, Uncomplexed actin
1QZ6 1.6 Å, Structure of rabbit actin in complex with jaspisamide A

Browse structure collections

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