8UEE: Actin, alpha skeletal muscle

Atomic structure of Salmonella SipA/F-actin complex by cryo-EM. Determined by electron microscopy at 3.2 Å resolution. Released 27 Dec 2023.

Method: Electron microscopy
Resolution: 3.2 Å
Organisms: Oryctolagus cuniculus, Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
Chains: 11
Atoms: 25,924
Mol. weight: 410.61 kDa
Ligands: PO4, MG, ADP
Released: 27 Dec 2023

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

Secondary structure: helices and β-sheets

8UEE contains 224 α-helices and 142 β-strands across 11 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: 14 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	520	1	39
α-helix	525-527	3
α-helix	530-531	2
α-helix	534-536	3
α-helix	542-553	12
α-helix	555	1
β-strand	556	1	39
α-helix	557	1
α-helix	562-575	14
α-helix	580-589	10
α-helix	593-595	3
α-helix	597-611	15
α-helix	616-629	14
α-helix	642-650	9
α-helix	656-658	3
α-helix	679-681	3

Chain B: 10 helices, 0 β-strands

Element	Residues	Length
α-helix	530-531	2
α-helix	532-535	4
α-helix	542-553	12
α-helix	562-575	14
α-helix	580-589	10
α-helix	599-611	13
α-helix	616-629	14
α-helix	641-650	10
α-helix	655-658	4
α-helix	677-681	5

Chain C: 12 helices, 0 β-strands

Element	Residues	Length
α-helix	530-531	2
α-helix	532-535	4
α-helix	542-553	12
α-helix	562-575	14
α-helix	580-589	10
α-helix	593-595	3
α-helix	597-610	14
α-helix	616-625	10
α-helix	626-630	5
α-helix	641-650	10
α-helix	655-657	3
α-helix	677-681	5

Chain D: 11 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	520	1	38
α-helix	534-536	3
α-helix	544-553	10
β-strand	556	1	38
α-helix	562-575	14
α-helix	581-590	10
α-helix	593-595	3
α-helix	597-611	15
α-helix	616-625	10
α-helix	626-630	5
α-helix	641-650	10
α-helix	655-657	3
α-helix	677-681	5

Chain F: 25 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	8-11	4	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
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	287-289	3
α-helix	290-294	5
β-strand	297-300	4	4
α-helix	302-305	4
α-helix	309-320	12
β-strand	329-330	2	4
α-helix	335-337	3
α-helix	338-348	11
α-helix	350-354	5
β-strand	357-358	2	1
α-helix	359-365	7
α-helix	367-369	3
α-helix	370-373	4

Chain H: 25 helices, 19 β-strands

Element	Residues	Length	Sheet
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
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
β-strand	103-107	5	6
α-helix	113-121	9
α-helix	122-126	5
β-strand	131-136	6	6
α-helix	137-144	8
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	193-195	3
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	287-289	3
α-helix	290-294	5
β-strand	297-300	4	9
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	9
α-helix	335-337	3
α-helix	338-348	11
α-helix	351-354	4
β-strand	357-358	2	6
α-helix	359-365	7
α-helix	367-369	3
α-helix	370-373	4

Chain I: 29 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	11
β-strand	16-21	6	11
β-strand	29-32	4	11
β-strand	35-37	3	12
α-helix	41	1
β-strand	42	1	9
β-strand	53-54	2	12
α-helix	57-60	4
α-helix	62-64	3
β-strand	66-68	3	12
α-helix	79-88	10
α-helix	89-93	5
α-helix	98-100	3
β-strand	105-107	3	13
α-helix	113-125	13
β-strand	131-132	2	14
β-strand	134-136	3	13
α-helix	137-144	8
β-strand	150-155	6	15
β-strand	160-166	7	15
β-strand	169-170	2	15
α-helix	172-174	3
β-strand	176-178	3	15
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	16
β-strand	247-250	4	16
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-267	4
α-helix	272-273	2
α-helix	274-283	10
α-helix	287-289	3
α-helix	290-294	5
β-strand	297-300	4	15
α-helix	302-305	4
α-helix	309-320	12
α-helix	326-327	2
β-strand	329-330	2	15
α-helix	335-337	3
α-helix	338-348	11
α-helix	350-352	3
β-strand	357-358	2	14
α-helix	359-365	7
α-helix	366-368	3
α-helix	369-373	5

Chain J: 23 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	17
β-strand	16-21	6	17
β-strand	29-32	4	17
β-strand	35-38	4	18
β-strand	42	1	4
β-strand	53-54	2	18
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	18
β-strand	71-72	2	19
β-strand	75-76	2	19
α-helix	79-88	10
α-helix	89-93	5
α-helix	98-100	3
β-strand	103-107	5	17
α-helix	113-122	10
α-helix	123-127	5
β-strand	131-136	6	17
α-helix	137-143	7
β-strand	150-155	6	20
β-strand	160-166	7	20
β-strand	169-170	2	20
α-helix	172-174	3
β-strand	176-178	3	20
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	21
β-strand	247-250	4	21
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	20
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	20
α-helix	338-348	11
β-strand	357-358	2	17
α-helix	359-365	7
α-helix	369-372	4

3 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	F, H, I, J, K, L, M	protein	375	Oryctolagus cuniculus	P68135 (AlphaFold model)
Cell invasion protein SipA	A, B, C, D	protein	261	Salmonella enterica subsp. enterica serovar Typhimurium str. LT2	P0CL52 (AlphaFold model)

Sequence of entity 1 (F, H, I, J, K, L, M), FASTA

>8UEE_1 Actin, alpha skeletal muscle (chains F, H, I, J, K, L, M)
DEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQS
KRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMT
QIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDL
AGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSY
ELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMS
GGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQ
EYDEAGPSIVHRKCF

Sequence of entity 2 (A, B, C, D), FASTA

>8UEE_2 Cell invasion protein SipA (chains A, B, C, D)
TGETTSFDEVDGVTSKSIIGKPVQATVHGVDDNKQQSQTAEIVNVKPLASQLAGVENVKT
DTLQSDTTVITGNKAGTTDNDNSQTDKTGPFSGLKFKQNSFLSTVPSVTNMHSMHFDARE
TFLGVIRKALEPDTSTPFPVRRAFDGLRAEILPNDTIKSAALKAQCSDIDKHPELKAKME
TLKEVITHHPQKEKLAEIALQFAREAGLTRLKGETDYVLSNVLDGLIGDGSWRAGPAYES
YLNKPGVDRVITTVDGLHMQR

Ligands and cofactors

ID	Name	Formula	Copies
PO4	Phosphate ion	O4 P	7
MG	Magnesium ion	Mg	7
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	7

Primary citation

Stabilization of F-actin by Salmonella effector SipA resembles the structural effects of inorganic phosphate and phalloidin. Niedzialkowska, E., Runyan, L.A., Kudryashova, E. et al. Structure (2024) 32:725-738.e8. DOI 10.1016/j.str.2024.02.022 · 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

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