8C4C: F-actin decorated by SipA497-669

F-actin decorated by SipA497-669. Determined by electron microscopy at 2.7 Å resolution. Released 17 Jan 2024.

Method: Electron microscopy
Resolution: 2.7 Å
Organisms: Gallus gallus, Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
Chains: 12
Atoms: 28,300
Mol. weight: 417.83 kDa
Ligands: ADP, PO4, MG
Released: 17 Jan 2024

Explore 8C4C in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8C4C contains 240 α-helices and 171 β-strands across 12 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: 23 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	8	1	1
β-strand	16	1	2
β-strand	19	1	3
β-strand	21	1	1
β-strand	29	1	3
β-strand	32	1	2
β-strand	35-38	4	4
β-strand	53-54	2	4
α-helix	62-64	3
β-strand	65-68	4	4
β-strand	71-72	2	5
β-strand	75-76	2	5
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	137-145	9
β-strand	150-155	6	6
β-strand	160-165	6	6
β-strand	170	1	6
α-helix	172-174	3
β-strand	176-178	3	6
α-helix	185-194	10
α-helix	204-216	13
α-helix	223-232	10
β-strand	238-241	4	7
β-strand	247-250	4	7
α-helix	253-259	7
α-helix	264-267	4
α-helix	272-273	2
α-helix	274-281	8
α-helix	287-294	8
β-strand	297-300	4	6
α-helix	302-305	4
α-helix	309-318	10
β-strand	329-330	2	6
α-helix	335-337	3
α-helix	338-348	11
α-helix	351-354	4
α-helix	356	1
β-strand	357-358	2	1
α-helix	359-365	7
α-helix	367-372	6

Chain B: 22 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	8-11	4	8
β-strand	16-21	6	8
β-strand	29-32	4	8
β-strand	35-38	4	9
β-strand	53-54	2	9
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	9
β-strand	71-72	2	10
β-strand	75-76	2	10
α-helix	79-87	9
α-helix	88-93	6
β-strand	103-107	5	8
α-helix	113-121	9
α-helix	122-126	5
β-strand	131-136	6	8
α-helix	137-145	9
β-strand	150-155	6	11
β-strand	160-166	7	11
β-strand	169-170	2	11
α-helix	172-174	3
β-strand	176-178	3	11
α-helix	182-193	12
α-helix	203-205	3
α-helix	206-216	11
α-helix	223-232	10
β-strand	238-241	4	12
β-strand	247-250	4	12
α-helix	253-262	10
α-helix	272-273	2
α-helix	274-284	11
α-helix	290-294	5
β-strand	297-300	4	11
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	11
α-helix	338-347	10
α-helix	350-354	5
β-strand	357-358	2	8
α-helix	359-365	7
α-helix	369-373	5

Chain C: 25 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	13
β-strand	16-21	6	13
β-strand	29-32	4	13
β-strand	35-38	4	14
β-strand	41	1	6
β-strand	53-54	2	14
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	14
β-strand	71-72	2	15
β-strand	75-76	2	15
α-helix	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	13
α-helix	113-125	13
β-strand	131-136	6	13
α-helix	137-145	9
β-strand	150-155	6	16
β-strand	160-166	7	16
β-strand	169-170	2	16
α-helix	172-174	3
β-strand	176-178	3	16
α-helix	182-193	12
α-helix	194-196	3
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	17
β-strand	247-250	4	17
α-helix	253-262	10
α-helix	264-267	4
α-helix	272-273	2
α-helix	274-284	11
α-helix	290-294	5
β-strand	297-300	4	16
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	16
α-helix	335-337	3
α-helix	338-348	11
α-helix	350-352	3
β-strand	357-358	2	13
α-helix	359-365	7
α-helix	366-368	3
α-helix	369-373	5

Chain D: 23 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	18
β-strand	16-21	6	18
β-strand	29-32	4	18
β-strand	35-38	4	19
β-strand	41	1	11
β-strand	53-54	2	19
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	19
β-strand	71-72	2	20
β-strand	75-76	2	20
α-helix	79-87	9
α-helix	88-94	7
α-helix	98-100	3
β-strand	103-107	5	18
α-helix	113-125	13
β-strand	131-136	6	18
α-helix	137-145	9
β-strand	150-155	6	21
β-strand	160-166	7	21
β-strand	169-170	2	21
α-helix	172-174	3
β-strand	176-178	3	21
α-helix	182-193	12
α-helix	194-196	3
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	22
β-strand	247-250	4	22
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-267	4
α-helix	274-284	11
α-helix	290-294	5
β-strand	297-300	4	21
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	21
α-helix	338-348	11
α-helix	350-355	6
β-strand	357-358	2	18
α-helix	359-365	7
α-helix	369-373	5

Chain E: 22 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	23
β-strand	16-21	6	23
β-strand	29-32	4	23
β-strand	35-38	4	24
β-strand	41	1	16
β-strand	53-54	2	24
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	24
β-strand	71-72	2	25
β-strand	75-76	2	25
α-helix	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	23
α-helix	113-125	13
β-strand	131-136	6	23
α-helix	137-145	9
β-strand	150-155	6	26
β-strand	160-166	7	26
β-strand	169-170	2	26
α-helix	172-174	3
β-strand	176-178	3	26
α-helix	182-193	12
α-helix	194-196	3
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	27
β-strand	247-250	4	27
α-helix	253-259	7
α-helix	264-267	4
α-helix	274-283	10
α-helix	290-294	5
β-strand	297-300	4	26
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	26
α-helix	338-348	11
α-helix	350-352	3
β-strand	357-358	2	23
α-helix	359-365	7
α-helix	369-373	5

Chain F: 23 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	28
β-strand	16-21	6	28
β-strand	29-32	4	28
β-strand	35-38	4	29
β-strand	41	1	21
β-strand	53-54	2	29
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	29
β-strand	71-72	2	30
β-strand	75-76	2	30
α-helix	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	28
α-helix	113-125	13
β-strand	131-136	6	28
α-helix	137-145	9
β-strand	150-155	6	31
β-strand	160-166	7	31
β-strand	169-170	2	31
α-helix	172-174	3
β-strand	176-178	3	31
α-helix	182-193	12
α-helix	194-196	3
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	32
β-strand	247-250	4	32
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	31
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	31
α-helix	338-347	10
α-helix	350-354	5
β-strand	357-358	2	28
α-helix	359-365	7
α-helix	369-373	5

Chain G: 24 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	33
β-strand	16-21	6	33
β-strand	22	1	34
β-strand	24	1	34
β-strand	29-32	4	33
β-strand	35-38	4	35
β-strand	41	1	26
β-strand	53-54	2	35
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	35
β-strand	71-72	2	36
β-strand	75-76	2	36
α-helix	79-87	9
α-helix	88-94	7
α-helix	98-100	3
β-strand	103-107	5	33
α-helix	113-121	9
α-helix	122-126	5
β-strand	131-136	6	33
α-helix	137-145	9
β-strand	150-155	6	37
β-strand	160-166	7	37
β-strand	169-170	2	37
α-helix	172-174	3
β-strand	176-178	3	37
α-helix	182-193	12
α-helix	194-196	3
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	38
β-strand	247-250	4	38
α-helix	253-259	7
α-helix	264-267	4
α-helix	274-284	11
α-helix	290-294	5
β-strand	297-300	4	37
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	37
α-helix	338-347	10
α-helix	350-354	5
β-strand	357-358	2	33
α-helix	359-365	7
α-helix	367-369	3
α-helix	370-373	4

Chain H: 21 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	8-11	4	39
β-strand	16-21	6	39
β-strand	29-32	4	39
β-strand	35-38	4	40
β-strand	41	1	31
β-strand	53-54	2	40
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	40
β-strand	71-72	2	41
β-strand	75-76	2	41
α-helix	79-87	9
α-helix	88-94	7
β-strand	103-107	5	39
α-helix	113-125	13
β-strand	131-136	6	39
α-helix	137-145	9
β-strand	150-155	6	42
β-strand	160-166	7	42
β-strand	169-170	2	42
α-helix	172-174	3
β-strand	176-178	3	42
α-helix	182-193	12
α-helix	194-196	3
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	43
β-strand	247-250	4	43
α-helix	253-259	7
α-helix	264-267	4
α-helix	274-283	10
α-helix	287-294	8
β-strand	297-300	4	42
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	42
α-helix	338-347	10
α-helix	351-354	4
β-strand	357-358	2	39
α-helix	359-365	7
α-helix	369-373	5

4 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Actin, alpha skeletal muscle	A, B, C, D, E, F, G, H	protein	377	Gallus gallus	P68139 (AlphaFold model)
Cell invasion protein SipA	K, L, M, N	protein	173	Salmonella enterica subsp. enterica serovar Typhimurium str. LT2	P0CL52 (AlphaFold model)

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

>8C4C_1 Actin, alpha skeletal muscle (chains A, B, C, D, E, F, G, H)
MCDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEA
QSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREK
MTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRL
DLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEK
SYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNV
MSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWIT
KQEYDEAGPSIVHRKCF

Sequence of entity 2 (K, L, M, N), FASTA

>8C4C_2 Cell invasion protein SipA (chains K, L, M, N)
NKAGTTDNDNSQTDKTGPFSGLKFKQNSFLSTVPSVTNMHSMHFDARETFLGVIRKALEP
DTSTPFPVRRAFDGLRAEILPNDTIKSAALKAQCSDIDKHPELKAKMETLKEVITHHPQK
EKLAEIALQFAREAGLTRLKGETDYVLSNVLDGLIGDGSWRAGPAYESYLNKP

Ligands and cofactors

ID	Name	Formula	Copies
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	8
PO4	Phosphate ion	O4 P	8
MG	Magnesium ion	Mg	8

Primary citation

Structural basis for subversion of host cell actin cytoskeleton during Salmonella infection. Yuan, B., Scholz, J., Wald, J. et al. Sci Adv (2023) 9:eadj5777-eadj5777. DOI 10.1126/sciadv.adj5777 · 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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