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- EMDB-35301: Structure of mammalian spectrin-actin junctional complex of membr... -

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Basic information

Entry
Database: EMDB / ID: EMD-35301
TitleStructure of mammalian spectrin-actin junctional complex of membrane skeleton, State I, Global map
Map data
Sample
  • Complex: Spectrin-actin junctional complex
    • Protein or peptide: x 10 types
  • Ligand: x 1 types
KeywordsMacrocomplex / membrane skeleton / spectrin-actin junction / MEMBRANE PROTEIN
Function / homology
Function and homology information


NCAM signaling for neurite out-growth / RAF/MAP kinase cascade / regulation of cellular component size / lens fiber cell development / endoplasmic reticulum tubular network organization / smooth endoplasmic reticulum calcium ion homeostasis / pointed-end actin filament capping / negative regulation of protein targeting to membrane / regulation of multicellular organismal development / positive regulation of developmental process ...NCAM signaling for neurite out-growth / RAF/MAP kinase cascade / regulation of cellular component size / lens fiber cell development / endoplasmic reticulum tubular network organization / smooth endoplasmic reticulum calcium ion homeostasis / pointed-end actin filament capping / negative regulation of protein targeting to membrane / regulation of multicellular organismal development / positive regulation of developmental process / spectrin / 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 / RHOF GTPase cycle / Formation of the canonical BAF (cBAF) complex / Formation of the polybromo-BAF (pBAF) complex / Formation of the embryonic stem cell BAF (esBAF) complex / Formation of the non-canonical BAF (ncBAF) complex / GBP-mediated host defense / Platelet degranulation / Striated Muscle Contraction / Gap junction degradation / Formation of annular gap junctions / UCH proteinases / spectrin-associated cytoskeleton / negative regulation of substrate adhesion-dependent cell spreading / Clathrin-mediated endocytosis / cuticular plate / Regulation of CDH1 Function / Formation of the dystrophin-glycoprotein complex (DGC) / myofibril assembly / positive regulation of cellular component organization / platelet dense tubular network membrane / cell projection membrane / negative regulation of focal adhesion assembly / regulation of filopodium assembly / cellular response to cytochalasin B / COP9 signalosome / regulation of transepithelial transport / morphogenesis of a polarized epithelium / structural constituent of postsynaptic actin cytoskeleton / protein localization to adherens junction / dense body / regulation of lamellipodium assembly / Tat protein binding / actin filament capping / postsynaptic actin cytoskeleton / positive regulation of fibroblast migration / apical protein localization / adherens junction assembly / RHO GTPases activate IQGAPs / RHO GTPases Activate Formins / tight junction / COPI-mediated anterograde transport / ankyrin binding / cortical actin cytoskeleton / positive regulation of wound healing / apical junction complex / spectrin binding / tropomyosin binding / erythrocyte development / NuA4 histone acetyltransferase complex / regulation of norepinephrine uptake / transporter regulator activity / smooth endoplasmic reticulum / cortical cytoskeleton / establishment or maintenance of cell polarity / myofibril / nitric-oxide synthase binding / striated muscle thin filament / brush border / regulation of synaptic vesicle endocytosis / kinesin binding / regulation of protein localization to plasma membrane / microtubule-based process / positive regulation of double-strand break repair via homologous recombination / axonogenesis / cytoskeleton organization / cell projection / muscle contraction / cellular response to cAMP / calyx of Held / cell motility / nitric-oxide synthase regulator activity / actin filament organization / actin filament / adherens junction / SH3 domain binding / synapse organization / cell junction / Schaffer collateral - CA1 synapse / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / structural constituent of cytoskeleton / cytoplasmic ribonucleoprotein granule / regulation of cell shape
Similarity search - Function
SH3-binding, glutamic acid-rich protein / : / SH3-binding, glutamic acid-rich protein / Putative adherens-junction anchoring domain / : / : / Putative adherens-junction anchoring region of AbLIM / Tropomodulin / Spectrin, beta subunit / Tropomodulin ...SH3-binding, glutamic acid-rich protein / : / SH3-binding, glutamic acid-rich protein / Putative adherens-junction anchoring domain / : / : / Putative adherens-junction anchoring region of AbLIM / Tropomodulin / Spectrin, beta subunit / Tropomodulin / TMOD/LMOD Leucine-rich domain / Class II aldolase/adducin N-terminal / Class II Aldolase and Adducin N-terminal domain / Class II Aldolase and Adducin N-terminal domain / Villin headpiece / Villin headpiece domain superfamily / Villin headpiece domain / Headpiece (HP) domain profile. / Villin headpiece domain / Class II aldolase/adducin N-terminal domain superfamily / EF-hand, Ca insensitive / Ca2+ insensitive EF hand / Ca2+ insensitive EF hand / Tropomyosins signature. / Tropomyosin / Tropomyosin / Spectrin repeat / Spectrin repeat / Spectrin/alpha-actinin / Spectrin repeats / DNA repair protein XRCC4-like, C-terminal / Actinin-type actin-binding domain signature 1. / Actinin-type actin-binding domain signature 2. / Actinin-type actin-binding domain, conserved site / Calponin homology domain / Calponin homology (CH) domain / Calponin homology domain / CH domain superfamily / Calponin homology (CH) domain profile. / Actins signature 1. / Actin, conserved site / Actins signature 2. / Actin/actin-like conserved site / Actins and actin-related proteins signature. / Actin / Actin family / Actin / SH3 domain / Leucine-rich repeat domain superfamily / Src homology 3 domains / SH3-like domain superfamily / Src homology 3 (SH3) domain profile. / SH3 domain / ATPase, nucleotide binding domain / EF-hand calcium-binding domain profile. / EF-hand domain / EF-hand domain pair / Thioredoxin-like superfamily
Similarity search - Domain/homology
Tropomodulin 1 / Spectrin beta chain / Beta-adducin / SH3 domain-binding glutamic acid-rich-like protein / Spectrin alpha chain, erythrocytic 1 / Dematin / Alpha-adducin / Tropomyosin alpha-4 chain / Actin, cytoplasmic 1
Similarity search - Component
Biological speciesSus scrofa (pig)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.6 Å
AuthorsLi N / Chen S / Gao N
Funding support China, 1 items
OrganizationGrant numberCountry
National Science Foundation (NSF, China) China
CitationJournal: Cell / Year: 2023
Title: Structural basis of membrane skeleton organization in red blood cells.
Authors: Ningning Li / Siyi Chen / Kui Xu / Meng-Ting He / Meng-Qiu Dong / Qiangfeng Cliff Zhang / Ning Gao /
Abstract: The spectrin-based membrane skeleton is a ubiquitous membrane-associated two-dimensional cytoskeleton underneath the lipid membrane of metazoan cells. Mutations of skeleton proteins impair the ...The spectrin-based membrane skeleton is a ubiquitous membrane-associated two-dimensional cytoskeleton underneath the lipid membrane of metazoan cells. Mutations of skeleton proteins impair the mechanical strength and functions of the membrane, leading to several different types of human diseases. Here, we report the cryo-EM structures of the native spectrin-actin junctional complex (from porcine erythrocytes), which is a specialized short F-actin acting as the central organizational unit of the membrane skeleton. While an α-/β-adducin hetero-tetramer binds to the barbed end of F-actin as a flexible cap, tropomodulin and SH3BGRL2 together create an absolute cap at the pointed end. The junctional complex is strengthened by ring-like structures of dematin in the middle actin layers and by patterned periodic interactions with tropomyosin over its entire length. This work serves as a structural framework for understanding the assembly and dynamics of membrane skeleton and offers insights into mechanisms of various ubiquitous F-actin-binding factors in other F-actin systems.
History
DepositionFeb 8, 2023-
Header (metadata) releaseMay 3, 2023-
Map releaseMay 3, 2023-
UpdateJul 2, 2025-
Current statusJul 2, 2025Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_35301.png

Downloads & links

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Map

FileDownload / File: emd_35301.map.gz / Format: CCP4 / Size: 421.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

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AxesZ (Sec.)Y (Row.)X (Col.)
1.37 Å/pix.
x 480 pix.
= 657.6 Å		1.37 Å/pix.
x 480 pix.
= 657.6 Å		1.37 Å/pix.
x 480 pix.
= 657.6 Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.37 Å
Density

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Histogram (log scale)
Contour LevelBy AUTHOR: 0.35
Minimum - Maximum-1.1503513 - 2.8394969
Average (Standard dev.)0.0019484502 (±0.070627145)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions480480480
Spacing480480480
CellA=B=C: 657.6 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #2

Fileemd_35301_half_map_1.map
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Half map: #1

Fileemd_35301_half_map_2.map
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Sample components

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Entire : Spectrin-actin junctional complex

EntireName: Spectrin-actin junctional complex
Components
  • Complex: Spectrin-actin junctional complex
    • Protein or peptide: Adducin 1
    • Protein or peptide: Beta-adducin
    • Protein or peptide: Dematin actin binding protein
    • Protein or peptide: Spectrin alpha, erythrocytic 1
    • Protein or peptide: Actin, cytoplasmic 1
    • Protein or peptide: Spectrin beta chain
    • Protein or peptide: Tropomyosin-1.9
    • Protein or peptide: Tropomyosin 3
    • Protein or peptide: Tropomodulin-1
    • Protein or peptide: SH3 domain-binding glutamic acid-rich-like protein
  • Ligand: ADENOSINE-5'-DIPHOSPHATE

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Supramolecule #1: Spectrin-actin junctional complex

SupramoleculeName: Spectrin-actin junctional complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#10
Source (natural)Organism: Sus scrofa (pig)

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Macromolecule #1: Adducin 1

MacromoleculeName: Adducin 1 / type: protein_or_peptide / ID: 1 / Number of copies: 3 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 81.307211 KDa
SequenceString: MNGDTRAAVV TSPPPTTAPH KERYFDRVDE NNPEYLRERN MAPDLRQDFN MMEQKKRVSM ILQSPAFCEE LESMIQEQFK KGKNPTGLL ALQQIADFMT TNVPNVYPAA PQGGMAALNM SLGMVTPVND LRGSDSIAYD KGEKLLRCKL AALYRLADLF G WSHLIYNH ...String:
MNGDTRAAVV TSPPPTTAPH KERYFDRVDE NNPEYLRERN MAPDLRQDFN MMEQKKRVSM ILQSPAFCEE LESMIQEQFK KGKNPTGLL ALQQIADFMT TNVPNVYPAA PQGGMAALNM SLGMVTPVND LRGSDSIAYD KGEKLLRCKL AALYRLADLF G WSHLIYNH ITTRVSSEQE HFLIVPFGLL YSEVTASSLV KINLQGDVVD RGSTNLGVNQ AGFTLHSAVY AARPDVKCVV HI HTPAGAA VSAMKCGLLP ISPEALSLGE VAYHDYHGIL VDEEEKVLIQ KNLGPKSKVL ILRNHGLVSV GESVEEAFYY IHN LVVACE IQVRTLASAG GPDNLVLLDP GKYKAKSRPP TSPAGEGSGS PPAWQIGEQE FEALMRMLDN LGYRTGYPYR YPAL REKSK KYSDVEVPAS VTGYSVASDG DSGTGSPLRH SFQKQQREKT RWLNSGRGDD ASEEGQAGSS PKSKTKWTKE DGHRA SASA VPNLFVPLNT NPKEVQEMRN KIREQNLQDI KTAGPQSQVL CGVVMDRSLV QGELVTASKA IIEKEYQPHV VVSTTG PNP FNTLTDRELE EYRREVERKQ KGPEETLDER SDQKEDSPPE PPAAPHTPPS TPVKLEEDLP QEPLSGDDSE AATFRPT LP DLPPDEPSEV LGFPTLEEEE EEEEVGALCE AGRPPSPARP AAEASPEPAA AQAAEEPASP AAEEGAAADP GSDGSPGK S PSKKKKKFRT PSFLKKSKKR SDS

UniProtKB: Alpha-adducin

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Macromolecule #2: Beta-adducin

MacromoleculeName: Beta-adducin / type: protein_or_peptide / ID: 2 / Number of copies: 3 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 80.705914 KDa
SequenceString: MSEETVPEAA SPPPAQGRQY FDRFSEEDPE YLRLRNRAAD LRQDFNLMEQ KKRVTMILQS PSFREELEGL IQEQMKKGNN SSNIWALRQ IADFMASTSH AVFPTSSMNF SMMTPINDLH TADSLNLAKG ERLMRCKISS VYRLLDLYGW AQLSDTYVTL R VSKEQDHF ...String:
MSEETVPEAA SPPPAQGRQY FDRFSEEDPE YLRLRNRAAD LRQDFNLMEQ KKRVTMILQS PSFREELEGL IQEQMKKGNN SSNIWALRQ IADFMASTSH AVFPTSSMNF SMMTPINDLH TADSLNLAKG ERLMRCKISS VYRLLDLYGW AQLSDTYVTL R VSKEQDHF LISPKGVSCS EVTASSLIKV NILGEVVEKG SSCFPVDTTG FCLHSAIYAA RPDVRCIIHL HTPATAAVSA MK WGLLPVS HNALLVGDMA YFDFNGEMEQ EADRINLQKC LGPTCKILVL RNHGVVALGD TVEEAFYKVF HLQAACEIQV SAL SSAGGV ENLILLEQEK HRPHEVGSVQ WAGSTFGPMQ KSRLGEHEFE ALMRMLDNLG YRTGYPYRYP LVQEKTKHKS EVEI PATVT AFVFEEDGAP VPALRQHAQK QQKEKTRWLN TPNTYLRVNV ADEVQRSMGS PRPKTTWMKA DEVEKSSSGM PIRIE NPNQ FVPLYTDPQE VLDMRNKIRE QNRQDVKSAG PQSQLLASVI AEKSRSPSTE SQLMSQGQAD TKDESEETVP NPFSQL TDQ ELEEYKKEVE RKKLELDGEK EPAVEEPGSP GKSAPASPAQ SPAKSETKSP VGSPSKSVDE EAQKTEPSKP TTEPETT QP EGVVVNGRED EPTAEEILSK GLSQMTTHAD TDVDTSKDKT ESVTSGPMSP EGSPSKSPSK KKKKFRTPSF LKKSKKKE K VES

UniProtKB: Beta-adducin

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Macromolecule #3: Dematin actin binding protein

MacromoleculeName: Dematin actin binding protein / type: protein_or_peptide / ID: 3 / Number of copies: 3 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 45.569348 KDa
SequenceString: MERLQKQPLT SPGSVSSSRG SSVPGSPSSI VAKMDNQVLG YKDLAAIPKD KAILDIERPD LMIYEPHFTY SLLEHVELPR SRERSLSPK STSPPPSPEV WAESRSPGTF PQASAPRTTG TPRTSLPHFH HPETTRPDSN IYKKPPIYKQ REPTGGSPQS K HLIEDLII ...String:
MERLQKQPLT SPGSVSSSRG SSVPGSPSSI VAKMDNQVLG YKDLAAIPKD KAILDIERPD LMIYEPHFTY SLLEHVELPR SRERSLSPK STSPPPSPEV WAESRSPGTF PQASAPRTTG TPRTSLPHFH HPETTRPDSN IYKKPPIYKQ REPTGGSPQS K HLIEDLII ESSKFPAAQP PDPNQPAKIE TDYWPCPPSL AVVETEWRKR KASRRGAEEE EEEEDDDSGE EMKALRERQR EE LSKVTSN LGKMILKEEM EKSLPIRRKT RSLPDRTPFH TSLQAGTSKS SSLPAYGRTT LSRLQSTDFS PSGSETESPG LQN GEGQRG RMDRGTSLPC VLEQKIYPYE MLVVTNKGRT KLPPGVDRMR LERHLSAEDF SRVFSMSPEE FGKLALWKRN ELKK KASLF

UniProtKB: Dematin

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Macromolecule #4: Spectrin alpha, erythrocytic 1

MacromoleculeName: Spectrin alpha, erythrocytic 1 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 281.361031 KDa
SequenceString: MNAGNWSQAM DSGGPKVLET AEEIQERRQE VLSRYGKFKE QVAERGQKLE DSYHYQVFKR DADDLKKWIL EKLKIAEDKS YEDPTNIQG KYQKHESFET EVQAKSRVIP ELEEIRRVRF TEGHVAHEDT KVLLEELHTL WNRLLEWTQQ KGSLLLQALK L QQYLQECA ...String:
MNAGNWSQAM DSGGPKVLET AEEIQERRQE VLSRYGKFKE QVAERGQKLE DSYHYQVFKR DADDLKKWIL EKLKIAEDKS YEDPTNIQG KYQKHESFET EVQAKSRVIP ELEEIRRVRF TEGHVAHEDT KVLLEELHTL WNRLLEWTQQ KGSLLLQALK L QQYLQECA DILEWIGDKE AIVTSEELGE DWERTEVLHK KFEEFQADLE IRRGRVNGVN QYADECVEEN HPKLPLIQSR RE EVNEAWE RLNKLASQRQ KSLSSVADLQ RFKRDVTEAI QWIKEKEPQL TSEDYGKDLF TSEALFHSHK GLERNLAVMD DKV KELCAK ADKLKLSHPS DADQIQQMKE DLVSNWEHIR TLATRRYEKL QASYWYQRFL SDYDELSGWM KEKTALINAD ELPT DVAGG EALLDRHQQH KHEIDSYDDR FQSAHETGQA LLDANHEASD EVMEKMNILV HTRAALLELW NRRQQQYEQC LNLHL FYRD SEQVDSWMSR QEAFLENEDL GNSLGSVEAL LQKHDDFEEA FTAQEEKITT LDETATKLID DHHYDSKNIA AIRDEL LAR QDALRKRAAT RRKLLEDSFL LQQLYQDSDD LKNWINKKKK LADDEDYKDT QNLKSQVQKQ QVFEEELAAN KILLDNL KQ TGQEMIENNH YASERVAARL SDIDSLWREL LEATAQKGTQ LYEANRLLQF ENNAEDLQRW LEEVKWQAFS EDYGKGLA D IQNLRRKHQL LESAVAARQD QADTLKDLAA HFEEIGHPNA GELRARQESL VSRFEELKEP LSFRKNKLND QFMLLWICR DTEDEEAWIQ ETEPSAASTY LGKDLIAAKK FLSRHQVIQA DIANHEPRIQ EITWRGNKMV EEGHFAAEDV ASRIKSLNEN MESLQARAA RRQNALEANV QFQQYLADLH EAEAWIREKE PIVDNTNYGA DEEAAGALLK KHEAFLVDLK AFGNSIQALR D QAEACQQQ QAAPVEADAR EERVMALYDF EARSPREVTM KKDDILILLS SINEDWWKVE ADDHQGFVPA NYVRKLAHDE FP MLPQRRR EEPENISQRQ EQIENQYHSL LDRAEERRRR LLQRYNEFLL AYEAGDMLDW IREKKAENTG VELDDVWELQ KKF DEFQTD LKTNEPRLRD INKVADDLLF EGLLTPEGTQ IQQELNARWG SLQRLAEEQR QLLGSAHAVQ MFHRDADDTK EQIE KKCQA LSAADPGSDL FSVQALQRQH EGFERDLTPL GEKVNILGET ANRLSESHPD ATDDLQRQRL ELKEAWEDLL GHTED RKEN LQEALKFYLF LSQARDLQNW ISGIGGMVSS QELAEDLTGT EILIERHQEQ RDEIEAEAPT FQVLEDFGRD LISSGH RAS PEIEEKLQTV RLERDELEKA WEQRKKMLDQ CLELQLFRVD CDQAENWMVA RENYLSSDDK GSLDSLGALM KKCDDLD KA ITTQDKKITE LELFAERLIA DDHYAQEEIA VRLQRILDRW KALKAQLIAE RTKLGDSADL KQFYRDLEDL NEWISEML P TACDESYKDT TNIQRKYLKH KTFENEVHGR TEEVEGVINL GNALVERRAC DGNEETVKGQ VEELEKEWNH LLERTADKG QKLNEASRQQ RFNTGIRDFE FWLSEAETLL SMKDQARDLA SAGNLLKKHQ LLETEMLARK DALKDLDTLA TDLISSGTFN TEQIVEKRD NVNKRFLNVE QLSAEHHEKL KEDYALFQFF QDLDNEEFWI EEKLVQVRSQ DYGRDLHGVQ NLLKKHKRLE G ELVAHEPA IQNVLDMAAT LGDKTTVGRE AIQERLDQFV QHWEQLKELT KARGFQLGES LEYLEFMENA EEEEAWLSEQ ET MVAQGDS GDSLATTQSL LKKLEALEND FAAHEIQVQN VCAQGRDILS KEESQHKEEI ATKIEALNEK TPSLAKAIAA WKS RLEDDH SFQQFNWKAD VVETWIAEKE TSLKTNGNGA DLAAFLTLLA KQDTLDATLQ SFQQERLSEI TDLKDQLVTA EHNQ TKAIE ERHAALLRRW EQLLEASEAH RQKLLEKQLP LQKAEDLFME FAHKASAFNN WCENVEEDLS EPVHCVSLDA IRQLQ KDHE AFLSSLARAQ SDFNYLLELD QQIKALNVPS SPYTWLTVEA LERIWKHLSD IIKEREQELE KEEARQVKNF EMCQEF EQN ASAFLNWILE TRAYFLDGSL LKETGTLESQ LEANKRKQKE IQAMKRQLTK IEDLGEKLEE ALVLDIKFST IGLAQQW DQ LFQLGVRRQH NLEQQIQIRD TPGVSEETLE EFKTTYRHFD ENLTGRLSHK DFRSCLRGLN YYLPMVEEGE SEPKFEKF L DAVDPGRKGY VTQEDYTYFL IDKESENIKS SDEIENSFQA LAEGKAYITK EDMKQALTPE QVSFCASHMQ QYVDPRGRS HPAGYDYVGF INSYFGN

UniProtKB: Spectrin alpha chain, erythrocytic 1

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Macromolecule #5: Actin, cytoplasmic 1

MacromoleculeName: Actin, cytoplasmic 1 / type: protein_or_peptide / ID: 5 / Number of copies: 12 / 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 #6: Spectrin beta chain

MacromoleculeName: Spectrin beta chain / type: protein_or_peptide / ID: 6 / Number of copies: 8 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 248.510672 KDa
SequenceString: MTSATEFENV GNQPPYSRIN ARWDAPDDEL DNDNSSARLF ERSRIKALAD EREVVQKKTF TKWVNSHLAR VSCRITDLYK DLRDGRMLI KLLEVLSGEM LPKPTKGKMR IHCLENVDKA LQFLKEQRVH LENMGSHDIV DGNHRLVLGL IWTIILRFQI Q DIVVQTQE ...String:
MTSATEFENV GNQPPYSRIN ARWDAPDDEL DNDNSSARLF ERSRIKALAD EREVVQKKTF TKWVNSHLAR VSCRITDLYK DLRDGRMLI KLLEVLSGEM LPKPTKGKMR IHCLENVDKA LQFLKEQRVH LENMGSHDIV DGNHRLVLGL IWTIILRFQI Q DIVVQTQE GRETRSAKDA LLLWCQMKTA GYPNVNVTNF TSSWKDGLAF NALIHKHRPD LIDFDKLKDS NARHNLEHAF DV AERQLGI IQLLDPEDVF TENPDEKSII TYVVAFYHYF SKMKVLAVEG KRVGKVIDHA IETEKMIEKY SGLASDLLTW IEQ TITVLN SRKFANSLAG VQQQLQAFST YRTVEKPPKF QEKGNLEVLL FTIQSRMRAN NQKVYTPHDG KLVSDINRAW ESLE EAEYR RELALRSELI RQEKLEQLAR RFDRKAAMRE TWLNENQRLV AQDNFGYDLA AVEAAKKKHE AIETDTAAYE ERVRA LEDL ARELELENYH DQKRITARKD NILRLWNYLQ ELLQSRRQRL ETTLALQQLF QDMLHSIDWM DEIKAHLLSA EFGKHL LEA EDLLQKHKLM EADIAIQGDK VKAITAATLQ FTEETGYQPC DPQVIRDRVS HLEQCFAELS NTAAGRKAQL EQSKRLW KL FWEMDEAKSW IKEKEQIYSS LGYGKDLTSV LILQRKHKAF EDELRRLDPH LDQIFQEAED MVALKQFGYP KNEAWVKE V SAQWDQLKEV PAQWNQLKEL AASRKKNLQD TENFFQFQGD VDDLKAWLQD AHKLLSGEDV GQDEGATRAL GKKHKDFLE ELEESRGVME HLEQQAQDFP ERFRDSPDVT NRLQVLRDLY QQVVAQADLR RQRLQDALDL YTVFGETDAC ELWMGEKEKW LAQMDIPDT LEDLEVVQHR FDILDQEMKT LIAQIDGVNV AANSLVESNH PRSTEVKQYQ DHLNTRWREF QTMVLARREA V DSALRVHN YCVDCEETSK WIIDKTKVVE STKDLGQDLA GVMAIQRKLS GLERDVAAIQ VRVGALEQES HRLMESHREQ EK DIGERQA YVEELWQGLQ QALKGQEALL GKSSQLQAFL QDLDAFEAWL STAQKEVASK DMPESLPEAE QLLQQHAALK DDI DRHQEN YQHVKASGEK VIHGQTDPEY LLLGQRLEGL DKGWDALCRM WESRGHTLAQ CLGFQEFQKD AKQAEAILSN QEYT LAHLE PPDSLEAAEA GIRKFQDFFT TMENNRDKVL SPVDSGNKLV AEGNLYSDKI KEKVQQIEDR HKRNNEKAQE ASVLL QDNL ALQNFLQNCQ ELTLWINDKL LTSQDVSYDD ARNLHNKWLK HTAFEAELAS QQGWLENIDA EGKQLMEEKP QFEALV SQR LEALHRLWDE LQATTKEIGQ RLSAARSSDL RSQTHADLNK WIRAMEDQLR SDDLGKDLTS VNRMLAKLKR VEDQVNV RK EELGELFAHM PSPGEEAEDE DLSIEKRFLD LLEPLGRRKK QLESSKAKLQ ISRDLEDETL WVEERLPLAQ STDYGANL Q TVQLFMKKNQ TLQNEILGHA PRVEDVLYRG HQLVEAAEID CQDIEERLGH LQNSWDTLQE AAAGRLQRLW DASEAQQYY LDAGEAEAWI SEQELYVISD EMPQDEEGAI VMLKRHLRQQ RMVEEYERNI KQLAGRAQSL LAAGHPEGEQ IIRLQGQVDK HYAGLKDMA EDRKRKLENK YRQFQMEREA DDLEQWILEK DLVASSPEMG QDFDHVTLLR DKFRDFARET GAIGQERVDN M NALIEHLI DAGHEEAASI AERKDGLNEM WADVLELIDT RMQLLAASYD RHRYFYTGNE ILGLIDEKHR ELPEDVGLDA ST AESFHRV HTAFERELHQ LGVQVQQFQD VATRLQAAYA GEEADSIQNK EQEVSAAWQA LLDACAGRRT QLVDTADKFR FFS MVRDLL SWMETIIRQI ETQERPRDVS SVELLMKYHQ GIWAEMDTRS KNFSACLELG ESLLQRQHQA SDEIREKLQQ VVSK KKEID EKWKARSDRL SMLLEVCQFS RDASVAEAWL IAQEPYLSSR DFGHTVDSVE KLIKRHEAFE KSTASWEPRF AALEK PTTL ELKERQTPER PKEDAGPQEE EGETAGEAPR GPHRAATERT SPVSSLSHLS SSWESLLPEP AHPY

UniProtKB: Spectrin beta chain

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Macromolecule #7: Tropomyosin-1.9

MacromoleculeName: Tropomyosin-1.9 / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 28.791223 KDa
SequenceString: MAGSSSLEAV RRKIRSLQEQ ADAAEERAGT LQRELDYERK LRETAEADVA SLNRRIQLVE EELDRAQERL ATALQKLEEA EKAADESER GMKVIESRAQ KDEEKMEIQE IQLKEAKHIA EDADRKYEEV ARKLVIIESD LERAEERAEL SEGQVRQLEE Q LRIMDQTL ...String:
MAGSSSLEAV RRKIRSLQEQ ADAAEERAGT LQRELDYERK LRETAEADVA SLNRRIQLVE EELDRAQERL ATALQKLEEA EKAADESER GMKVIESRAQ KDEEKMEIQE IQLKEAKHIA EDADRKYEEV ARKLVIIESD LERAEERAEL SEGQVRQLEE Q LRIMDQTL KALMAAEDKY SQKEDKYEEE IKVLSDKLKE AETRAEFAER SVTKLEKSID DLEEKVAHAK EENLSMHQML DQ TLLELNN M

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Macromolecule #8: Tropomyosin 3

MacromoleculeName: Tropomyosin 3 / type: protein_or_peptide / ID: 8 / Number of copies: 3 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 29.080742 KDa
SequenceString: MAGITTIEAV KRKIQVLQQQ ADDAEERAER LQREVEGERR AREQAEAEVA SLNRRIQLVE EELDRAQERL ATALQKLEEA EKAADESER GMKVIENRAL KDEEKMELQE IQLKEAKHIA EEADRKYEEV ARKLVIIEGD LERTEERAEL AESRCREMDE Q IRLMDQNL ...String:
MAGITTIEAV KRKIQVLQQQ ADDAEERAER LQREVEGERR AREQAEAEVA SLNRRIQLVE EELDRAQERL ATALQKLEEA EKAADESER GMKVIENRAL KDEEKMELQE IQLKEAKHIA EEADRKYEEV ARKLVIIEGD LERTEERAEL AESRCREMDE Q IRLMDQNL KCLSAAEEKY SQKEDKYEEE IKILTDKLKE AETRAEFAER SVAKLEKTID DLEDKLKCTK EEHLCTQRML DQ TLLDLNE M

UniProtKB: Tropomyosin alpha-4 chain

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Macromolecule #9: Tropomodulin-1

MacromoleculeName: Tropomodulin-1 / type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 40.523055 KDa
SequenceString: MSYRRELEKY RDLDEDEILG ALTEEELRTL ENELDELDPD NALLPAGLRQ KDQTTKAPTG PFKREELLDH LEKQAKEFKD REDLVPYTG EKRGKVWVPK QKPMDPVLET VTLEPELEEA LANASDAELC DIAAILGMHT LMSNQQYYQA LGSSSIVNKE G LNSVIKPT ...String:
MSYRRELEKY RDLDEDEILG ALTEEELRTL ENELDELDPD NALLPAGLRQ KDQTTKAPTG PFKREELLDH LEKQAKEFKD REDLVPYTG EKRGKVWVPK QKPMDPVLET VTLEPELEEA LANASDAELC DIAAILGMHT LMSNQQYYQA LGSSSIVNKE G LNSVIKPT QYKPVPDEEP NATDVEETLE RIKNNDPKLE EVNLNNIRNI PIPTLKAYAE ALKENSYVKK FSIVGTRSND PV AFALAEM LKVNKVLKTL NVESNFISGA GILRLVEALP YNTSLVELKI DNQSQPLGNK VEMEIVSMLE KNATLLKFGY HFT QQGPRL RASNAMMNNN DLVRKRRLAD LTGPIIPKCR SGI

UniProtKB: Tropomodulin 1

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Macromolecule #10: SH3 domain-binding glutamic acid-rich-like protein

MacromoleculeName: SH3 domain-binding glutamic acid-rich-like protein / type: protein_or_peptide / ID: 10 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 12.28593 KDa
SequenceString:
MVIRVFIASS SGFVAIKKKQ QDVVRFLEAN KIEFEEVDIT MSEEQRQWMY KNIPPEKKPA QGNPLPPQIF NGDRYCGDYD SFFESKESN TVFSFLGLKS QLASKAEP

UniProtKB: SH3 domain-binding glutamic acid-rich-like protein

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Macromolecule #11: ADENOSINE-5'-DIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 11 / 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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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.5
VitrificationCryogen name: ETHANE / Chamber humidity: 100 %

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K2 QUANTUM (4k x 4k) / Detector mode: SUPER-RESOLUTION / Average electron dose: 34.4 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.0 µm / Nominal defocus min: 2.0 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

+
Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.6 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 43000
Initial angle assignmentType: PROJECTION MATCHING
Final angle assignmentType: PROJECTION MATCHING
FSC plot (resolution estimation)

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