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- EMDB-17558: Cryo-EM structure of cortactin stabilized Arp2/3-complex nucleate... -

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Basic information

Entry
Database: EMDB / ID: EMD-17558
TitleCryo-EM structure of cortactin stabilized Arp2/3-complex nucleated actin branches
Map data
Sample
  • Complex: Cortactin stabilizes Arp2/3-complex nucleated actin branches with daughter filament capped
    • Complex: Human Arp2/3 C1BC5L complex
      • Protein or peptide: x 7 types
    • Complex: Porcine actin, cytoplasmic 1
      • Protein or peptide: x 1 types
    • Complex: Mouse cortactin
      • Protein or peptide: x 1 types
    • Complex: Mouse capping protein
      • Protein or peptide: x 2 types
    • Complex: Phalloidin
      • Protein or peptide: x 1 types
  • Ligand: x 2 types
KeywordsComplex / CONTRACTILE PROTEIN
Function / homology
Function and homology information


cytoskeletal calyx / tubulobulbar complex / meiotic chromosome movement towards spindle pole / cytosolic transport / growth cone leading edge / muscle cell projection membrane / meiotic cytokinesis / lamellipodium organization / Advanced glycosylation endproduct receptor signaling / RHOF GTPase cycle ...cytoskeletal calyx / tubulobulbar complex / meiotic chromosome movement towards spindle pole / cytosolic transport / growth cone leading edge / muscle cell projection membrane / meiotic cytokinesis / lamellipodium organization / Advanced glycosylation endproduct receptor signaling / RHOF GTPase cycle / spindle localization / RHOD GTPase cycle / Gap junction degradation / Formation of annular gap junctions / Regulation of actin dynamics for phagocytic cup formation / EPHB-mediated forward signaling / Adherens junctions interactions / VEGFA-VEGFR2 Pathway / Cell-extracellular matrix interactions / RHO GTPases Activate WASPs and WAVEs / MAP2K and MAPK activation / UCH proteinases / Clathrin-mediated endocytosis / RHOF GTPase cycle / site of polarized growth / actin polymerization-dependent cell motility / COPI-independent Golgi-to-ER retrograde traffic / Arp2/3 protein complex / asymmetric cell division / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / Arp2/3 complex-mediated actin nucleation / WASH complex / Arp2/3 complex binding / : / actin nucleation / F-actin capping protein complex / COPI-mediated anterograde transport / negative regulation of filopodium assembly / modification of postsynaptic actin cytoskeleton / modification of postsynaptic structure / mitotic spindle midzone / regulation of cell projection assembly / actin cap / regulation of mitophagy / postsynaptic actin cytoskeleton / profilin binding / structural constituent of postsynaptic actin cytoskeleton / Factors involved in megakaryocyte development and platelet production / dense body / positive regulation of smooth muscle contraction / regulation of actin filament polymerization / positive regulation of chemotaxis / substrate-dependent cell migration, cell extension / cell projection organization / MHC class II antigen presentation / cell junction assembly / barbed-end actin filament capping / actin polymerization or depolymerization / focal adhesion assembly / regulation of cell morphogenesis / podosome / proline-rich region binding / regulation of lamellipodium assembly / RHO GTPases activate IQGAPs / RHO GTPases Activate Formins / dendritic spine maintenance / lamellipodium assembly / regulation of axon extension / establishment or maintenance of cell polarity / cortical actin cytoskeleton / cortical cytoskeleton / positive regulation of actin filament polymerization / NuA4 histone acetyltransferase complex / filamentous actin / brush border / positive regulation of double-strand break repair via homologous recombination / asymmetric synapse / cilium assembly / RHO GTPases Activate WASPs and WAVEs / positive regulation of lamellipodium assembly / extrinsic apoptotic signaling pathway / clathrin-coated pit / positive regulation of substrate adhesion-dependent cell spreading / voltage-gated potassium channel complex / ruffle / cytoskeleton organization / EPHB-mediated forward signaling / hippocampal mossy fiber to CA3 synapse / actin filament polymerization / axonogenesis / neuron projection morphogenesis / receptor-mediated endocytosis / cellular response to nerve growth factor stimulus / cell projection / negative regulation of extrinsic apoptotic signaling pathway / cell motility / actin filament / FCGR3A-mediated phagocytosis / intracellular protein transport / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement
Similarity search - Function
Hs1/Cortactin / Cortactin, SH3 domain / Repeat in HS1/Cortactin / Cortactin repeat profile. / Actin-related protein 2/3 complex subunit 5 / Actin-related protein 2/3 complex subunit 2 / Actin-related protein 2/3 complex subunit 3 / Actin-related protein 2/3 complex subunit 4 / Actin-related protein 2/3 complex subunit 1 / Arp2/3 complex subunit 2/4 ...Hs1/Cortactin / Cortactin, SH3 domain / Repeat in HS1/Cortactin / Cortactin repeat profile. / Actin-related protein 2/3 complex subunit 5 / Actin-related protein 2/3 complex subunit 2 / Actin-related protein 2/3 complex subunit 3 / Actin-related protein 2/3 complex subunit 4 / Actin-related protein 2/3 complex subunit 1 / Arp2/3 complex subunit 2/4 / Actin-related protein 2/3 complex subunit 5 superfamily / Actin-related protein 2/3 complex subunit 3 superfamily / Arp2/3 complex, 34 kD subunit p34-Arc / ARP2/3 complex ARPC3 (21 kDa) subunit / ARP2/3 complex 16 kDa subunit (p16-Arc) / ARP2/3 complex 20 kDa subunit (ARPC4) / F-actin-capping protein subunit beta / F-actin capping protein, beta subunit, conserved site / F-actin-capping protein subunit beta, N-terminal domain / F-actin capping protein, beta subunit / F-actin capping protein beta subunit signature. / F-actin capping protein, alpha subunit, conserved site / F-actin capping protein alpha subunit signature 1. / F-actin capping protein alpha subunit signature 2. / F-actin-capping protein subunit alpha / F-actin-capping protein subunit alpha/beta / F-actin-capping protein subunit alpha/beta, domain 2 / F-actin capping protein, alpha subunit, domain 1 / F-actin capping protein alpha subunit / Variant SH3 domain / Actins signature 1. / Actin, conserved site / Actins signature 2. / Actin/actin-like conserved site / Actins and actin-related proteins signature. / Actin / Actin family / Actin / ATPase, nucleotide binding domain / Src homology 3 domains / SH3-like domain superfamily / Src homology 3 (SH3) domain profile. / SH3 domain / Trp-Asp (WD) repeats profile. / Trp-Asp (WD) repeats circular profile. / WD domain, G-beta repeat / WD40 repeats / WD40 repeat / WD40-repeat-containing domain superfamily / WD40/YVTN repeat-like-containing domain superfamily
Similarity search - Domain/homology
Actin-related protein 2/3 complex subunit 1B / Actin-related protein 2/3 complex subunit 2 / Actin-related protein 2/3 complex subunit 3 / F-actin-capping protein subunit alpha-1 / F-actin-capping protein subunit beta / Actin-related protein 2/3 complex subunit 4 / Actin-related protein 3 / Actin-related protein 2 / Src substrate cortactin / Actin, cytoplasmic 1 / Actin-related protein 2/3 complex subunit 5-like protein
Similarity search - Component
Biological speciesHomo sapiens (human) / Sus scrofa (pig) / Mus musculus (house mouse) / Amanita phalloides (death cap)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.3 Å
AuthorsLiu T / Moores CA
Funding supportEuropean Union, 1 items
OrganizationGrant numberCountry
European Research Council (ERC)810207European Union
CitationJournal: Nat Struct Mol Biol / Year: 2024
Title: Cortactin stabilizes actin branches by bridging activated Arp2/3 to its nucleated actin filament.
Authors: Tianyang Liu / Luyan Cao / Miroslav Mladenov / Antoine Jegou / Michael Way / Carolyn A Moores /
Abstract: Regulation of the assembly and turnover of branched actin filament networks nucleated by the Arp2/3 complex is essential during many cellular processes, including cell migration and membrane ...Regulation of the assembly and turnover of branched actin filament networks nucleated by the Arp2/3 complex is essential during many cellular processes, including cell migration and membrane trafficking. Cortactin is important for actin branch stabilization, but the mechanism by which this occurs is unclear. Given this, we determined the structure of vertebrate cortactin-stabilized Arp2/3 actin branches using cryogenic electron microscopy. We find that cortactin interacts with the new daughter filament nucleated by the Arp2/3 complex at the branch site, rather than the initial mother actin filament. Cortactin preferentially binds activated Arp3. It also stabilizes the F-actin-like interface of activated Arp3 with the first actin subunit of the new filament, and its central repeats extend along successive daughter-filament subunits. The preference of cortactin for activated Arp3 explains its retention at the actin branch and accounts for its synergy with other nucleation-promoting factors in regulating branched actin network dynamics.
History
DepositionJun 5, 2023-
Header (metadata) releaseJan 3, 2024-
Map releaseJan 3, 2024-
UpdateMay 29, 2024-
Current statusMay 29, 2024Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_17558.png

Downloads & links

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Map

FileDownload / File: emd_17558.map.gz / Format: CCP4 / Size: 325 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 1.067 Å
Density
Contour LevelBy AUTHOR: 0.15
Minimum - Maximum-0.28256604 - 0.7510417
Average (Standard dev.)0.0013075767 (±0.024123373)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions440440440
Spacing440440440
CellA=B=C: 469.48 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #2

Fileemd_17558_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
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Histogram

Histogram (log scale)

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Half map: #1

Fileemd_17558_half_map_2.map
Projections & Slices
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Histogram

Histogram (log scale)

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Sample components

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Entire : Cortactin stabilizes Arp2/3-complex nucleated actin branches with...

EntireName: Cortactin stabilizes Arp2/3-complex nucleated actin branches with daughter filament capped
Components
  • Complex: Cortactin stabilizes Arp2/3-complex nucleated actin branches with daughter filament capped
    • Complex: Human Arp2/3 C1BC5L complex
      • Protein or peptide: Actin-related protein 3
      • Protein or peptide: Actin-related protein 2
      • Protein or peptide: Actin-related protein 2/3 complex subunit 1B
      • Protein or peptide: Actin-related protein 2/3 complex subunit 2
      • Protein or peptide: Actin-related protein 2/3 complex subunit 3
      • Protein or peptide: Actin-related protein 2/3 complex subunit 4
      • Protein or peptide: Actin-related protein 2/3 complex subunit 5-like protein
    • Complex: Porcine actin, cytoplasmic 1
      • Protein or peptide: Actin, cytoplasmic 1
    • Complex: Mouse cortactin
      • Protein or peptide: Src substrate cortactin
    • Complex: Mouse capping protein
      • Protein or peptide: F-actin-capping protein subunit alpha-1
      • Protein or peptide: Isoform 2 of F-actin-capping protein subunit beta
    • Complex: Phalloidin
      • Protein or peptide: Phalloidin
  • Ligand: ADENOSINE-5'-DIPHOSPHATE
  • Ligand: MAGNESIUM ION

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Supramolecule #1: Cortactin stabilizes Arp2/3-complex nucleated actin branches with...

SupramoleculeName: Cortactin stabilizes Arp2/3-complex nucleated actin branches with daughter filament capped
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#12
Source (natural)Organism: Homo sapiens (human)

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Supramolecule #2: Human Arp2/3 C1BC5L complex

SupramoleculeName: Human Arp2/3 C1BC5L complex / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1-#7
Source (natural)Organism: Homo sapiens (human)

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Supramolecule #3: Porcine actin, cytoplasmic 1

SupramoleculeName: Porcine actin, cytoplasmic 1 / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #8
Source (natural)Organism: Sus scrofa (pig)

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Supramolecule #4: Mouse cortactin

SupramoleculeName: Mouse cortactin / type: complex / ID: 4 / Parent: 1 / Macromolecule list: #9
Source (natural)Organism: Mus musculus (house mouse)

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Supramolecule #5: Mouse capping protein

SupramoleculeName: Mouse capping protein / type: complex / ID: 5 / Parent: 1 / Macromolecule list: #10-#11
Source (natural)Organism: Mus musculus (house mouse)

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Supramolecule #6: Phalloidin

SupramoleculeName: Phalloidin / type: complex / ID: 6 / Parent: 1 / Macromolecule list: #12
Source (natural)Organism: Amanita phalloides (death cap)

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Macromolecule #1: Actin-related protein 3

MacromoleculeName: Actin-related protein 3 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 47.428031 KDa
Recombinant expressionOrganism: unidentified baculovirus
SequenceString: MAGRLPACVV DCGTGYTKLG YAGNTEPQFI IPSCIAIKES AKVGDQAQRR VMKGVDDLDF FIGDEAIEKP TYATKWPIRH GIVEDWDLM ERFMEQVIFK YLRAEPEDHY FLLTEPPLNT PENREYTAEI MFESFNVPGL YIAVQAVLAL AASWTSRQVG E RTLTGTVI ...String:
MAGRLPACVV DCGTGYTKLG YAGNTEPQFI IPSCIAIKES AKVGDQAQRR VMKGVDDLDF FIGDEAIEKP TYATKWPIRH GIVEDWDLM ERFMEQVIFK YLRAEPEDHY FLLTEPPLNT PENREYTAEI MFESFNVPGL YIAVQAVLAL AASWTSRQVG E RTLTGTVI DSGDGVTHVI PVAEGYVIGS CIKHIPIAGR DITYFIQQLL RDREVGIPPE QSLETAKAVK ERYSYVCPDL VK EFNKYDT DGSKWIKQYT GINAISKKEF SIDVGYERFL GPEIFFHPEF ANPDFTQPIS EVVDEVIQNC PIDVRRPLYK NIV LSGGST MFRDFGRRLQ RDLKRTVDAR LKLSEELSGG RLKPKPIDVQ VITHHMQRYA VWFGGSMLAS TPEFYQVCHT KKDY EEIGP SICRHNPVFG VMS

UniProtKB: Actin-related protein 3

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Macromolecule #2: Actin-related protein 2

MacromoleculeName: Actin-related protein 2 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 44.818711 KDa
Recombinant expressionOrganism: unidentified baculovirus
SequenceString: MDSQGRKVVV CDNGTGFVKC GYAGSNFPEH IFPALVGRPI IRSTTKVGNI EIKDLMVGDE ASELRSMLEV NYPMENGIVR NWDDMKHLW DYTFGPEKLN IDTRNCKILL TEPPMNPTKN REKIVEVMFE TYQFSGVYVA IQAVLTLYAQ GLLTGVVVDS G DGVTHICP ...String:
MDSQGRKVVV CDNGTGFVKC GYAGSNFPEH IFPALVGRPI IRSTTKVGNI EIKDLMVGDE ASELRSMLEV NYPMENGIVR NWDDMKHLW DYTFGPEKLN IDTRNCKILL TEPPMNPTKN REKIVEVMFE TYQFSGVYVA IQAVLTLYAQ GLLTGVVVDS G DGVTHICP VYEGFSLPHL TRRLDIAGRD ITRYLIKLLL LRGYAFNHSA DFETVRMIKE KLCYVGYNIE QEQKLALETT VL VESYTLP DGRIIKVGGE RFEAPEALFQ PHLINVEGVG VAELLFNTIQ AADIDTRSEF YKHIVLSGGS TMYPGLPSRL ERE LKQLYL ERVLKGDVEK LSKFKIRIED PPRRKHMVFL GGAVLADIMK DKDNFWMTRQ EYQEKGVRVL EKLGVTVR

UniProtKB: Actin-related protein 2

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Macromolecule #3: Actin-related protein 2/3 complex subunit 1B

MacromoleculeName: Actin-related protein 2/3 complex subunit 1B / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 41.004781 KDa
Recombinant expressionOrganism: unidentified baculovirus
SequenceString: MAYHSFLVEP ISCHAWNKDR TQIAICPNNH EVHIYEKSGA KWTKVHELKE HNGQVTGIDW APESNRIVTC GTDRNAYVWT LKGRTWKPT LVILRINRAA RCVRWAPNEN KFAVGSGSRV ISICYFEQEN DWWVCKHIKK PIRSTVLSLD WHPNNVLLAA G SCDFKCRI ...String:
MAYHSFLVEP ISCHAWNKDR TQIAICPNNH EVHIYEKSGA KWTKVHELKE HNGQVTGIDW APESNRIVTC GTDRNAYVWT LKGRTWKPT LVILRINRAA RCVRWAPNEN KFAVGSGSRV ISICYFEQEN DWWVCKHIKK PIRSTVLSLD WHPNNVLLAA G SCDFKCRI FSAYIKEVEE RPAPTPWGSK MPFGELMFES SSSCGWVHGV CFSASGSRVA WVSHDSTVCL ADADKKMAVA TL ASETLPL LALTFITDNS LVAAGHDCFP VLFTYDAAAG MLSFGGRLDV PKQSSQRGLT ARERFQNLDK KASSEGGTAA GAG LDSLHK NSVSQISVLS GGKAKCSQFC TTGMDGGMSI WDVKSLESAL KDLKIK

UniProtKB: Actin-related protein 2/3 complex subunit 1B

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Macromolecule #4: Actin-related protein 2/3 complex subunit 2

MacromoleculeName: Actin-related protein 2/3 complex subunit 2 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 34.386043 KDa
Recombinant expressionOrganism: unidentified baculovirus
SequenceString: MILLEVNNRI IEETLALKFE NAAAGNKPEA VEVTFADFDG VLYHISNPNG DKTKVMVSIS LKFYKELQAH GADELLKRVY GSFLVNPES GYNVSLLYDL ENLPASKDSI VHQAGMLKRN CFASVFEKYF QFQEEGKEGE NRAVIHYRDD ETMYVESKKD R VTVVFSTV ...String:
MILLEVNNRI IEETLALKFE NAAAGNKPEA VEVTFADFDG VLYHISNPNG DKTKVMVSIS LKFYKELQAH GADELLKRVY GSFLVNPES GYNVSLLYDL ENLPASKDSI VHQAGMLKRN CFASVFEKYF QFQEEGKEGE NRAVIHYRDD ETMYVESKKD R VTVVFSTV FKDDDDVVIG KVFMQEFKEG RRASHTAPQV LFSHREPPLE LKDTDAAVGD NIGYITFVLF PRHTNASARD NT INLIHTF RDYLHYHIKC SKAYIHTRMR AKTSDFLKVL NRARPDAEKK EMKTITGKTF SSR

UniProtKB: Actin-related protein 2/3 complex subunit 2

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Macromolecule #5: Actin-related protein 2/3 complex subunit 3

MacromoleculeName: Actin-related protein 2/3 complex subunit 3 / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 20.572666 KDa
Recombinant expressionOrganism: unidentified baculovirus
SequenceString:
MPAYHSSLMD PDTKLIGNMA LLPIRSQFKG PAPRETKDTD IVDEAIYYFK ANVFFKNYEI KNEADRTLIY ITLYISECLK KLQKCNSKS QGEKEMYTLG ITNFPIPGEP GFPLNAIYAK PANKQEDEVM RAYLQQLRQE TGLRLCEKVF DPQNDKPSKW W TCFVKRQF MNKSLSGPGQ

UniProtKB: Actin-related protein 2/3 complex subunit 3

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Macromolecule #6: Actin-related protein 2/3 complex subunit 4

MacromoleculeName: Actin-related protein 2/3 complex subunit 4 / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 19.697047 KDa
Recombinant expressionOrganism: unidentified baculovirus
SequenceString:
MTATLRPYLS AVRATLQAAL CLENFSSQVV ERHNKPEVEV RSSKELLLQP VTISRNEKEK VLIEGSINSV RVSIAVKQAD EIEKILCHK FMRFMMMRAE NFFILRRKPV EGYDISFLIT NFHTEQMYKH KLVDFVIHFM EEIDKEISEM KLSVNARARI V AEEFLKNF

UniProtKB: Actin-related protein 2/3 complex subunit 4

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Macromolecule #7: Actin-related protein 2/3 complex subunit 5-like protein

MacromoleculeName: Actin-related protein 2/3 complex subunit 5-like protein
type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 16.96418 KDa
Recombinant expressionOrganism: unidentified baculovirus
SequenceString:
MARNTLSSRF RRVDIDEFDE NKFVDEQEEA AAAAAEPGPD PSEVDGLLRQ GDMLRAFHAA LRNSPVNTKN QAVKERAQGV VLKVLTNFK SSEIEQAVQS LDRNGVDLLM KYIYKGFEKP TENSSAVLLQ WHEKALAVGG LGSIIRVLTA RKTV

UniProtKB: Actin-related protein 2/3 complex subunit 5-like protein

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Macromolecule #8: Actin, cytoplasmic 1

MacromoleculeName: Actin, cytoplasmic 1 / type: protein_or_peptide / ID: 8 / Number of copies: 10 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 41.78266 KDa
SequenceString: MDDDIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS KRGILTLKYP IEHGIVTNWD DMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM TQIMFETFNT PAMYVAIQAV LSLYASGRTT GIVMDSGDGV T HTVPIYEG ...String:
MDDDIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS KRGILTLKYP IEHGIVTNWD DMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM TQIMFETFNT PAMYVAIQAV LSLYASGRTT GIVMDSGDGV T HTVPIYEG YALPHAILRL DLAGRDLTDY LMKILTERGY SFTTTAEREI VRDIKEKLCY VALDFEQEMA TAASSSSLEK SY ELPDGQV ITIGNERFRC PEALFQPSFL GMESCGIHET TFNSIMKCDV DIRKDLYANT VLSGGTTMYP GIADRMQKEI TAL APSTMK IKIIAPPERK YSVWIGGSIL ASLSTFQQMW ISKQEYDESG PSIVHRKCF

UniProtKB: Actin, cytoplasmic 1

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Macromolecule #9: Src substrate cortactin

MacromoleculeName: Src substrate cortactin / type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 61.340738 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MWKASAGHAV SITQDDGGAD DWETDPDFVN DVSEKEQRWG AKTVQGSGHQ EHINIHKLRE NVFQEHQTLK EKELETGPKA SHGYGGKFG VEQDRMDRSA VGHEYQSKLS KHCSQVDSVR GFGGKFGVQM DRVDQSAVGF EYQGKTEKHA SQKDYSSGFG G KYGVQADR ...String:
MWKASAGHAV SITQDDGGAD DWETDPDFVN DVSEKEQRWG AKTVQGSGHQ EHINIHKLRE NVFQEHQTLK EKELETGPKA SHGYGGKFG VEQDRMDRSA VGHEYQSKLS KHCSQVDSVR GFGGKFGVQM DRVDQSAVGF EYQGKTEKHA SQKDYSSGFG G KYGVQADR VDKSAVGFDY QGKTEKHESQ KDYSKGFGGK YGIDKDKVDK SAVGFEYQGK TEKHESQKDY VKGFGGKFGV QT DRQDKCA LGWDHQEKLQ LHESQKDYKT GFGGKFGVQS ERQDSSAVGF DYKERLAKHE SQQDYAKGFG GKYGVQKDRM DKN ASTFEE VVQVPSAYQK TVPIEAVTSK TSNIRANFEN LAKEREQEDR RKAEAERAQR MAKERQEQEE ARRKLEEQAR AKKQ TPPAS PSPQPIEDRP PSSPIYEDAA PFKAEPSYRG SEPEPEYSIE AAGIPEAGSQ QGLTYTSEPV YETTEAPGHY QAEDD TYDG YESDLGITAI ALYDYQAAGD DEISFDPDDI ITNIEMIDDG WWRGVCKGRY GLFPANYVEL RQ

UniProtKB: Src substrate cortactin

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Macromolecule #10: F-actin-capping protein subunit alpha-1

MacromoleculeName: F-actin-capping protein subunit alpha-1 / type: protein_or_peptide / ID: 10 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 32.980703 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MADFEDRVSD EEKVRIAAKF ITHAPPGEFN EVFNDVRLLL NNDNLLREGA AHAFAQYNMD QFTPVKIEGY DDQVLITEHG DLGNSRFLD PRNQISFKFD HLRKEASDPQ PEDVDGGLKS WRESCDSALR AYVKDHYSNG FCTVYAKTID GQQTIIACIE S HQFQPKNF ...String:
MADFEDRVSD EEKVRIAAKF ITHAPPGEFN EVFNDVRLLL NNDNLLREGA AHAFAQYNMD QFTPVKIEGY DDQVLITEHG DLGNSRFLD PRNQISFKFD HLRKEASDPQ PEDVDGGLKS WRESCDSALR AYVKDHYSNG FCTVYAKTID GQQTIIACIE S HQFQPKNF WNGRWRSEWK FTITPPSAQV VGVLKIQVHY YEDGNVQLVS HKDVQDSVTV SNEVQTTKEF IKIIESAENE YQ TAISENY QTMSDTTFKA LRRQLPVTRT KIDWNKILSY KIGKEMQNA

UniProtKB: F-actin-capping protein subunit alpha-1

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Macromolecule #11: Isoform 2 of F-actin-capping protein subunit beta

MacromoleculeName: Isoform 2 of F-actin-capping protein subunit beta / type: protein_or_peptide / ID: 11 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 30.669768 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MSDQQLDCAL DLMRRLPPQQ IEKNLSDLID LVPSLCEDLL SSVDQPLKIA RDKVVGKDYL LCDYNRDGDS YRSPWSNKYD PPLEDGAMP SARLRKLEVE ANNAFDQYRD LYFEGGVSSV YLWDLDHGFA GVILIKKAGD GSKKIKGCWD SIHVVEVQEK S SGRTAHYK ...String:
MSDQQLDCAL DLMRRLPPQQ IEKNLSDLID LVPSLCEDLL SSVDQPLKIA RDKVVGKDYL LCDYNRDGDS YRSPWSNKYD PPLEDGAMP SARLRKLEVE ANNAFDQYRD LYFEGGVSSV YLWDLDHGFA GVILIKKAGD GSKKIKGCWD SIHVVEVQEK S SGRTAHYK LTSTVMLWLQ TNKSGSGTMN LGGSLTRQME KDETVSDCSP HIANIGRLVE DMENKIRSTL NEIYFGKTKD IV NGLRSVQ TFADKSKQEA LKNDLVEALK RKQQC

UniProtKB: F-actin-capping protein subunit beta

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Macromolecule #12: Phalloidin

MacromoleculeName: Phalloidin / type: protein_or_peptide / ID: 12 / Number of copies: 10 / Enantiomer: LEVO
Source (natural)Organism: Amanita phalloides (death cap)
Molecular weightTheoretical: 808.899 Da
SequenceString:
W(EEP)A(DTH)C(HYP)A

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Macromolecule #13: ADENOSINE-5'-DIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 13 / Number of copies: 12 / Formula: ADP
Molecular weightTheoretical: 427.201 Da
Chemical component information

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

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Macromolecule #14: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 14 / Number of copies: 12 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.5
Details: 20 mM HEPES pH 7.5, 50mM KCl, 1mM EGTA, 1mM MgCl2, 0.2 mM ATP and 1 mM DTT
VitrificationCryogen name: ETHANE / Chamber humidity: 98 % / Chamber temperature: 295.15 K / Instrument: LEICA EM GP / Details: Back blotting.

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 49.4 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.4 µm / Nominal defocus min: 0.9 µm / Nominal magnification: 81000
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 2001580
Startup modelType of model: NONE / Details: CryoSPARC ab-intio reconstruction
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 130915
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial modelChain - Source name: AlphaFold / Chain - Initial model type: in silico model
RefinementProtocol: OTHER
Output model

PDB-8p94:
Cryo-EM structure of cortactin stabilized Arp2/3-complex nucleated actin branches

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