8TAH: Cortactin-bound to Arp2/3 complex

Cryo-EM structure of Cortactin-bound to Arp2/3 complex. Determined by electron microscopy at 2.89 Å resolution. Released 27 Sept 2023.

Method: Electron microscopy
Resolution: 2.89 Å
Organisms: Bos taurus, Mus musculus
Chains: 8
Atoms: 14,978
Mol. weight: 234.57 kDa
Ligands: MG, ATP
Released: 27 Sept 2023

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

Secondary structure: helices and β-sheets

8TAH contains 83 α-helices and 88 β-strands across 7 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: 25 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	6-7	2
β-strand	8-12	5	1
β-strand	16-21	6	1
β-strand	29-32	4	1
β-strand	35-38	4	2
α-helix	56-58	3
β-strand	60-62	3	2
α-helix	63-66	4
β-strand	72-75	4	2
β-strand	78-79	2	3
β-strand	82-83	2	3
α-helix	86-95	10
α-helix	96-101	6
β-strand	110-114	5	1
α-helix	120-134	15
β-strand	138-143	6	1
α-helix	144-151	8
β-strand	165-169	5	4
α-helix	174	1
β-strand	175-181	7	4
β-strand	184-185	2	4
α-helix	187-189	3
β-strand	191-193	3	4
α-helix	197-211	15
α-helix	220-231	12
α-helix	238-247	10
β-strand	254-259	6	5
β-strand	266-271	6	5
α-helix	274-277	4
α-helix	279-282	4
α-helix	285-287	3
α-helix	296-305	10
α-helix	312-317	6
β-strand	319-322	4	4
α-helix	324-326	3
α-helix	331-353	23
α-helix	360-362	3
β-strand	367-368	2	4
α-helix	376-385	10
α-helix	388-392	5
β-strand	395-396	2	1
α-helix	397-402	6
α-helix	405-408	4
α-helix	412-414	3

Chain B: 16 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	8-11	4	6
β-strand	17-22	6	6
β-strand	30-33	4	6
β-strand	37-38	2	7
β-strand	69-70	2	7
β-strand	74-75	2	8
β-strand	78-79	2	8
α-helix	82-93	12
β-strand	106-111	6	6
α-helix	117-129	13
β-strand	135-140	6	6
α-helix	141-148	8
β-strand	154-159	6	9
β-strand	164-170	7	9
β-strand	173-174	2	9
β-strand	180-182	3	9
α-helix	186-198	13
α-helix	210-220	11
α-helix	227-236	10
β-strand	242-245	4	10
β-strand	251-254	4	10
α-helix	257-260	4
α-helix	261-264	4
α-helix	268-271	4
α-helix	278-287	10
α-helix	294-298	5
β-strand	301-304	4	9
α-helix	306-308	3
α-helix	313-328	16
β-strand	344	1	9
α-helix	353-364	12
β-strand	373	1	6
α-helix	375-379	5
α-helix	384-387	4

Chain C: 3 helices, 30 β-strands

Element	Residues	Length	Sheet
β-strand	3-5	3	11
β-strand	14-16	3	12
β-strand	22-25	4	12
β-strand	32-37	6	12
β-strand	42-48	7	12
β-strand	55-61	7	13
β-strand	66-71	6	13
β-strand	76-80	5	13
β-strand	87-91	5	13
β-strand	99-104	6	13
β-strand	110-115	6	13
β-strand	120-126	7	13
β-strand	131-137	7	13
β-strand	145-150	6	14
β-strand	156-161	6	14
β-strand	166-170	5	14
β-strand	183	1	15
β-strand	186	1	15
β-strand	193-198	6	14
β-strand	207-212	6	16
β-strand	218-223	6	16
β-strand	227-232	6	16
β-strand	238-243	6	16
α-helix	248	1
β-strand	249-254	6	17
β-strand	259-264	6	17
β-strand	270-274	5	17
β-strand	280-285	6	17
α-helix	288-290	3
β-strand	327-332	6	11
β-strand	342-347	6	11
β-strand	351-356	6	11
α-helix	357-363	7

Chain D: 16 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	4-5	2
α-helix	9-24	16
β-strand	33-36	4	18
α-helix	38-40	3
β-strand	42-46	5	18
α-helix	48-50	3
β-strand	54-60	7	18
α-helix	64-68	5
α-helix	72-79	8
α-helix	81-83	3
β-strand	84	1	18
α-helix	86-88	3
β-strand	93-98	6	18
α-helix	107-113	7
α-helix	116-133	18
α-helix	139-141	3
β-strand	142-144	3	19
β-strand	151-156	6	19
β-strand	161-168	8	19
α-helix	172-186	15
α-helix	196	1
β-strand	197-202	6	19
α-helix	207-209	3
β-strand	220-227	8	19
α-helix	237-244	8
α-helix	247-278	32

Chain E: 8 helices, 4 β-strands

Element	Residues	Length	Sheet
β-strand	14	1	20
β-strand	21	1	20
α-helix	33-34	2
α-helix	41-52	12
α-helix	64-81	18
α-helix	88-99	12
α-helix	103-105	3
β-strand	106	1	21
β-strand	108	1	21
α-helix	118-120	3
α-helix	123-148	26
α-helix	168-170	3

Chain F: 8 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	6-19	14
α-helix	37-40	4
α-helix	44-46	3
β-strand	47	1	22
α-helix	48-50	3
β-strand	51-54	4	23
β-strand	60-65	6	23
β-strand	66	1	22
β-strand	69-75	7	23
α-helix	81-96	16
β-strand	104	1	23
α-helix	108-109	2
β-strand	114-119	6	23
α-helix	120-125	6
α-helix	128-166	39

Chain G: 7 helices, 0 β-strands

Element	Residues	Length
α-helix	39-47	9
α-helix	51-58	8
α-helix	69-84	16
α-helix	91-96	6
α-helix	100-113	14
α-helix	121-136	16
α-helix	139-145	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Actin-related protein 3	A	protein	418	Bos taurus	P61157 (AlphaFold model)
Actin-related protein 2	B	protein	394	Bos taurus	A7MB62 (AlphaFold model)
Actin-related protein 2/3 complex subunit 1A	C	protein	370	Bos taurus	Q1JP79 (AlphaFold model)
Actin-related protein 2/3 complex subunit 2	D	protein	300	Bos taurus	Q3MHR7 (AlphaFold model)
Actin-related protein 2/3 complex subunit 3	E	protein	178	Bos taurus	Q3T035
Actin-related protein 2/3 complex subunit 4	F	protein	168	Bos taurus	Q148J6
Actin-related protein 2/3 complex subunit 5	G	protein	151	Bos taurus	G3MXC8
Src substrate cortactin	H	protein	76	Mus musculus	Q60598

Sequence of entity 1 (A), FASTA

>8TAH_1 Actin-related protein 3 (chains A)
MAGRLPACVVDCGTGYTKLGYAGNTEPQFIIPSCIAIKESAKVGDQAQRRVMKGVDDLDF
FIGDEAIEKPTYATKWPIRHGIVEDWDLMERFMEQVIFKYLRAEPEDHYFLLTEPPLNTP
ENREYTAEIMFESFNVPGLYIAVQAVLALAASWTSRQVGERTLTGTVIDSGDGVTHVIPV
AEGYVIGSCIKHIPIAGRDITYFIQQLLRDREVGIPPEQSLETAKAVKERYSYVCPDLVK
EFNKYDTDGSKWIKQYTGINAISKKEFSIDVGYERFLGPEIFFHPEFANPDFTQPISEVV
DEVIQNCPIDVRRPLYKNIVLSGGSTMFRDFGRRLQRDLKRTVDARLKLSEELSGGRLKP
KPIDVQVITHHMQRYAVWFGGSMLASTPEFYQVCHTKKDYEEIGPSICRHNPVFGVMS

Sequence of entity 2 (B), FASTA

>8TAH_2 Actin-related protein 2 (chains B)
MDSQGRKVVVCDNGTGFVKCGYAGSNFPEHIFPALVGRPIIRSTTKVGNIEIKDLMVGDE
ASELRSMLEVNYPMENGIVRNWDDMKHLWDYTFGPEKLNIDTRNCKILLTEPPMNPTKNR
EKIVEVMFETYQFSGVYVAIQAVLTLYAQGLLTGVVVDSGDGVTHICPVYEGFSLPHLTR
RLDIAGRDITRYLIKLLLLRGYAFNHSADFETVRMIKEKLCYVGYNIEQEQKLALETTVL
VESYTLPDGRIIKVGGERFEAPEALFQPHLINVEGVGVAELLFNTIQAADIDTRSEFYKH
IVLSGGSTMYPGLPSRLERELKQLYLERVLKGDVEKLSKFKIRIEDPPRRKHMVFLGGAV
LADIMKDKDNFWMTRQEYQEKGVRVLEKLGVTVR

Sequence of entity 3 (C), FASTA

>8TAH_3 Actin-related protein 2/3 complex subunit 1A (chains C)
MSLHQFLLEPITCHAWNRDRTQIALSPNNHEVHIYKKNGGQWVKAHELKEHNGHITGIDW
APKSDRIVTCGADRNAYVWSQKDGVWKPTLVILRINRAATFVKWSPLENKFAVGSGARLI
SVCYFESENDWWVSKHIKKPIRSTVLSLDWHPNNVLLAAGSCDFKCRVFSAYIKEVDEKP
ASTPWGSKMPFGQLMSEFGGSGTGGWVHGVSFSASGSRLAWVSHDSTVSVADASKSVQVS
TLKTEFLPLLSVSFVSENSVVAAGHDCCPMLFNYDDRGCLTFVSKLDIPKQSIQRNMSAM
ERFRNMDKRATTEDRNTALETLHQNSITQVSIYEVDKQDCRKFCTTGIDGAMTIWDFKTL
ESSIQGLRIM

Sequence of entity 4 (D), FASTA

>8TAH_4 Actin-related protein 2/3 complex subunit 2 (chains D)
MILLEVNNRIIEETLALKFENAAAGNKPEAVEVTFADFDGVLYHISNPNGDKTKVMVSIS
LKFYKELQAHGADELLKRVYGSYLVNPESGYNVSLLYDLENLPASKDSIVHQAGMLKRNC
FASVFEKYFQFQEEGKEGENRAVIHYRDDETMYVESKKDRVTVVFSTVFKDDDDVVIGKV
FMQEFKEGRRASHTAPQVLFSHREPPLELKDTDAAVGDNIGYITFVLFPRHTNASARDNT
INLIHTFRDYLHYHIKCSKAYIHTRMRAKTSDFLKVLNRARPDAEKKEMKTITGKTFSSR

Sequence of entity 5 (E), FASTA

>8TAH_5 Actin-related protein 2/3 complex subunit 3 (chains E)
MPAYHSSLMDPDTKLIGNMALLPIRSQFKGPAPRETKDTDIVDEAIYYFKANVFFKNYEI
KNEADRTLIYITLYISECLKKLQKCNSKSQGEKEMYTLGITNFPIPGEPGFPLNAIYAKP
ANKQEDEVMRAYLQQLRQETGLRLCEKVFDPQNDKPSKWWTCFVKRQFMNKSLSGPGQ

Sequence of entity 6 (F), FASTA

>8TAH_6 Actin-related protein 2/3 complex subunit 4 (chains F)
MTATLRPYLSAVRATLQAALCLENFSSQVVERHNKPEVEVRSSKELLLQPVTISRNEKEK
VLIEGSINSVRVSIAVKQADEIEKILCHKFMRFMMMRAENFFILRRKPVEGYDISFLITN
FHTEQMYKHKLVDFVIHFMEEIDKEISEMKLSVNARARIVAEEFLKNF

Sequence of entity 7 (G), FASTA

>8TAH_7 Actin-related protein 2/3 complex subunit 5 (chains G)
MSKNTVSSARFRKVDVDEYDENKFVDEEDGGDGQAGPDEGEVDSCLRQGNMTAALQAALK
NPPINTKSQAVKDRAGSIVLKVLISFKANDIEKAVQSLDKNGVDLLMKYIYKGFESPSDN
SSAVLLQWHEKALAAGGVGSIVRVLTARKTV

Sequence of entity 8 (H), FASTA

>8TAH_8 Src substrate cortactin (chains H)
MWKASAGHAVSITQDDGGADDWETDPDFVNDVSEKEQRWGAKTVQGSGHQEHINIHKLRE
NVFQEHQTLKEKELET

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	2
ATP	Adenosine-5'-triphosphate	C10 H16 N5 O13 P3	2

Primary citation

Mechanism of synergistic activation of Arp2/3 complex by cortactin and WASP-family proteins. Fregoso, F.E., Boczkowska, M., Rebowski, G. et al. Nat Commun (2023) 14:6894-6894. DOI 10.1038/s41467-023-42229-y · PubMed

Other PDB entries of the same protein (UniProt P61157 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1K8K 2.0 Å, Crystal Structure of Arp2/3 Complex
2P9I 2.46 Å, Crystal Structure of bovine Arp2/3 Complex co-crystallized with ADP and crosslinked with…
3UKR 2.48 Å, Crystal structure of Bos taurus Arp2/3 complex with bound inhibitor CK-666
3ULE 2.5 Å, Structure of Bos taurus Arp2/3 complex with bound inhibitor CK-869 and ATP
1TYQ 2.55 Å, Crystal structure of Arp2/3 complex with bound ATP and calcium
1U2V 2.55 Å, Crystal structure of Arp2/3 complex with bound ADP and calcium
2P9K 2.59 Å, Crystal structure of bovine Arp2/3 complex co-crystallized with ATP and crosslinked with…
2P9L 2.65 Å, Crystal Structure of bovine Arp2/3 complex
3RSE 2.65 Å, Structural and biochemical characterization of two binding sites for nucleation…
2P9S 2.68 Å, Structure of bovine Arp2/3 complex co-crystallized with ATP/Mg2+
3DXK 2.7 Å, Structure of Bos Taurus Arp2/3 Complex with Bound Inhibitor CK0944636
2P9U 2.75 Å, Crystal structure of bovine Arp2/3 complex co-crystallized with AMP-PNP and calcium

Browse structure collections

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