7R8V: ADP state actin filament

Cryo-EM structure of the ADP state actin filament. Determined by electron microscopy at 2.82 Å resolution. Released 28 Jul 2021.

Method: Electron microscopy
Resolution: 2.82 Å
Organism: Gallus gallus
Chains: 5
Atoms: 14,845
Mol. weight: 209.19 kDa
Ligands: MG, ADP
Released: 28 Jul 2021

Explore 7R8V in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7R8V contains 115 α-helices and 98 β-strands across 5 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 and D: 23 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	7
β-strand	16-21	6	7
β-strand	29-32	4	7
β-strand	35-38	4	8
β-strand	41-42	2	5
β-strand	53-54	2	8
α-helix	56-60	5
β-strand	65-68	4	8
β-strand	71-72	2	9
β-strand	75-76	2	9
α-helix	79-87	9
α-helix	88-93	6
β-strand	103-107	5	7
α-helix	113-125	13
β-strand	131-136	6	7
α-helix	137-145	9
β-strand	150-155	6	10
β-strand	160-165	6	10
β-strand	170	1	10
α-helix	172-174	3
β-strand	176-178	3	10
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	11
β-strand	247-250	4	11
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	10
α-helix	302-305	4
α-helix	309-320	12
β-strand	329-330	2	10
α-helix	335-337	3
α-helix	338-347	10
α-helix	350-355	6
β-strand	357-358	2	7
α-helix	359-365	7
α-helix	366-368	3
α-helix	369-373	5

Chain B: 23 helices, 20 β-strands

Element	Residues	Length	Sheet
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	41-42	2	3
β-strand	53-54	2	2
α-helix	56-60	5
β-strand	65-68	4	2
β-strand	71-72	2	4
β-strand	75-76	2	4
α-helix	79-87	9
α-helix	88-93	6
β-strand	103-107	5	1
α-helix	113-125	13
β-strand	131-136	6	1
α-helix	137-145	9
β-strand	150-155	6	5
β-strand	160-165	6	5
β-strand	169-170	2	5
α-helix	172-174	3
β-strand	176-178	3	5
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	6
β-strand	247-250	4	6
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	5
α-helix	302-305	4
α-helix	309-320	12
β-strand	329-330	2	5
α-helix	335-337	3
α-helix	338-347	10
α-helix	350-355	6
β-strand	357-358	2	1
α-helix	359-365	7
α-helix	366-368	3
α-helix	369-373	5

Chains C and E: 23 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	12
β-strand	16-21	6	12
β-strand	29-32	4	12
β-strand	35-38	4	13
β-strand	53-54	2	13
α-helix	56-60	5
β-strand	65-68	4	13
β-strand	71-72	2	14
β-strand	75-76	2	14
α-helix	79-87	9
α-helix	88-93	6
β-strand	103-107	5	12
α-helix	113-125	13
β-strand	131-136	6	12
α-helix	137-145	9
β-strand	150-155	6	3
β-strand	160-165	6	3
β-strand	169-170	2	3
α-helix	172-174	3
β-strand	176-178	3	3
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	3
α-helix	302-305	4
α-helix	309-320	12
β-strand	329-330	2	3
α-helix	335-337	3
α-helix	338-347	10
α-helix	350-355	6
β-strand	357-358	2	12
α-helix	359-365	7
α-helix	366-368	3
α-helix	369-373	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Actin, alpha skeletal muscle, intermediate form	A, B, C, D, E	protein	371	Gallus gallus	P68139 (AlphaFold model)

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

>7R8V_1 Actin, alpha skeletal muscle, intermediate form (chains A, B, C, D, E)
TTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGI
LTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMF
ETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDLAGRD
LTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPD
GQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMSGGTT
MYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQEYDE
AGPSIVHRKCF

Ligands and cofactors

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

Primary citation

Structural basis for tunable control of actin dynamics by myosin-15 in mechanosensory stereocilia. Gong, R., Jiang, F., Moreland, Z.G. et al. Sci Adv (2022) 8:eabl4733-eabl4733. DOI 10.1126/sciadv.abl4733 · PubMed

Other PDB entries of the same protein (UniProt P68139 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7W4Z 1.15 Å, Crystal structure of fragmin domain-1 in complex with actin (AMPPNP-form)
7W50 1.15 Å, Crystal structure of fragmin domain-1 in complex with actin (ADP-Pi-form)
7W51 1.2 Å, Crystal structure of fragmin domain-1 in complex with actin (ADP-form)
9L2N 1.7 Å, Crystal structure of Cytochalasin D bound to a filamentous conformation actin
7W52 2.0 Å, Crystal structure of fragmin domain-1 (15-160) in complex with actin
1MDU 2.2 Å, Crystal structure of the chicken actin trimer complexed with human gelsolin segment 1…
8D13 2.43 Å, Helical ADP-F-actin
8D14 2.51 Å, Helical ADP-Pi-F-actin
7R94 2.6 Å, T-Plastin-F-actin complex
8C4E 2.6 Å, F-actin decorated by SipA426-685
9JW0 2.69 Å, Structure of the N-terminal 3 domains (V1-V3) villin bound to actin
7YNE 2.7 Å, Crystal structure of fragmin domain-1 (1-160) in complex with G-form actin

Browse structure collections

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