EMDB-46847: structure of dynactin, dynein tail with one BICDR from dynein-dyn...

Basic information

Entry

Database: EMDB / ID: EMD-46847

• Title: structure of dynactin, dynein tail with one BICDR from dynein-dynactin-BICDR on microtubules
• Map data: structure of dynactin, dynein tail with one BICDR from dynein-dynactin-BICDR on microtubules

Sample

• Complex: Dynactin, dynein tail with one BICDR of dynein-dynactin-BICDR complex on microtubules
  • Protein or peptide: x 15 types
• Ligand: x 3 types

• Keywords: dynein / dynactin / microtubule / MOTOR PROTEIN

Function / homology

Function:

Golgi to secretory granule transport / RHOD GTPase cycle / Factors involved in megakaryocyte development and platelet production / retrograde axonal transport of mitochondrion / 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 / Gap junction degradation / Formation of annular gap junctions / RHOF GTPase cycle / centriolar subdistal appendage / Clathrin-mediated endocytosis / Formation of the dystrophin-glycoprotein complex (DGC) / positive regulation of neuromuscular junction development / dynactin complex / centriole-centriole cohesion / Regulation of PLK1 Activity at G2/M Transition / Loss of Nlp from mitotic centrosomes / Loss of proteins required for interphase microtubule organization from the centrosome / Anchoring of the basal body to the plasma membrane / AURKA Activation by TPX2 / F-actin capping protein complex / WASH complex / microtubule anchoring at centrosome / Recruitment of mitotic centrosome proteins and complexes / ventral spinal cord development / retromer complex / cytoskeleton-dependent cytokinesis / microtubule plus-end / nuclear membrane disassembly / cellular response to cytochalasin B / positive regulation of microtubule nucleation / regulation of transepithelial transport / morphogenesis of a polarized epithelium / structural constituent of postsynaptic actin cytoskeleton / barbed-end actin filament capping / melanosome transport / protein localization to adherens junction / dense body / Neutrophil degranulation / postsynaptic actin cytoskeleton / Tat protein binding / coronary vasculature development / non-motile cilium assembly / regulation of cell morphogenesis / dynein complex / retrograde transport, endosome to Golgi / adherens junction assembly / apical protein localization / RHO GTPases activate IQGAPs / RHO GTPases Activate Formins / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / MHC class II antigen presentation / Recruitment of NuMA to mitotic centrosomes / tight junction / minus-end-directed microtubule motor activity / microtubule associated complex / cytoplasmic dynein complex / dynein light intermediate chain binding / centrosome localization / COPI-mediated anterograde transport / aorta development / ventricular septum development / neuromuscular process / microtubule-based movement / nuclear migration / apical junction complex / regulation of norepinephrine uptake / transporter regulator activity / neuromuscular junction development / nitric-oxide synthase binding / cortical cytoskeleton / NuA4 histone acetyltransferase complex / establishment or maintenance of cell polarity / dynein complex binding / cell leading edge / motor behavior / dynein intermediate chain binding / cleavage furrow / brush border / establishment of mitotic spindle orientation / dynactin binding / kinesin binding / regulation of synaptic vesicle endocytosis / regulation of protein localization to plasma membrane / positive regulation of double-strand break repair via homologous recombination / intercellular bridge / stress fiber / cytoskeleton organization / neuron projection maintenance / axon cytoplasm / centriole / axonogenesis / regulation of mitotic spindle organization / calyx of Held

Domain/homology:

Dynactin subunit 3 / Dynactin subunit p22 / : / Dynactin subunit 4 / Dynactin p62 family / Dynein associated protein / Dynein associated protein / Dynamitin / : / Dynamitin / Dynactin subunit 6 / Dynein 1 light intermediate chain / Dynactin subunit 5 / Dynein family light intermediate chain / Dynein light intermediate chain (DLIC) / Cytoplasmic dynein 1 intermediate chain 1/2 / Cytoplasmic dynein 1 intermediate chain 2 / 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 / CAP-Gly domain signature. / : / CAP Gly-rich domain / CAP Gly-rich domain superfamily / CAP-Gly domain / CAP-Gly domain profile. / CAP_GLY / Dynein heavy chain, AAA 5 extension domain / Dynein heavy chain AAA lid domain / Dynein heavy chain, C-terminal domain / Dynein heavy chain, C-terminal domain, barrel region / Dynein heavy chain C-terminal domain / : / Dynein heavy chain, ATPase lid domain / Dynein heavy chain, tail / Dynein heavy chain, N-terminal region 1 / P-loop containing dynein motor region / Dynein heavy chain region D6 P-loop domain / Dynein heavy chain, linker / Dynein heavy chain, AAA module D4 / Dynein heavy chain, coiled coil stalk / Dynein heavy chain / Dynein heavy chain, hydrolytic ATP-binding dynein motor region / Dynein heavy chain, ATP-binding dynein motor region / Dynein heavy chain AAA lid domain / Dynein heavy chain AAA lid domain superfamily / Dynein heavy chain, domain 2, N-terminal / Dynein heavy chain, linker, subdomain 3 / Dynein heavy chain, AAA1 domain, small subdomain / Dynein heavy chain region D6 P-loop domain / Dynein heavy chain, N-terminal region 2 / Hydrolytic ATP binding site of dynein motor region / Microtubule-binding stalk of dynein motor / P-loop containing dynein motor region D4 / ATP-binding dynein motor region / Dynein heavy chain AAA lid domain / Trimeric LpxA-like superfamily / 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 / WD domain, G-beta repeat / WD40 repeats / WD40 repeat / WD40-repeat-containing domain superfamily / WD40/YVTN repeat-like-containing domain superfamily / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase

Component:

Dynactin subunit 5 / Dynactin subunit 1 / Cytoplasmic dynein 1 heavy chain 1 / Dynactin subunit 4 / Cytoplasmic dynein 1 intermediate chain 2 / Dynactin subunit 2 / Dynein light intermediate chain / Alpha-centractin / BICD family-like cargo adapter 1 / F-actin-capping protein subunit alpha-1 / F-actin-capping protein subunit beta / Dynactin subunit 6 / Dynactin subunit 3 / Actin-related protein 10 / Actin, cytoplasmic 1

• Biological species: Sus scrofa (pig) / Mus musculus (house mouse)
• Method: single particle reconstruction / cryo EM / Resolution: 7.2 Å
• Authors: Rao Q / Chai P / Zhang K

Funding support

United States, 1 items

Organization	Grant number	Country
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)	R35 GM142959	United States

• Citation: Journal: To Be Published; Title: Structure of dynein-dynactin on microtubules; Authors: Rao Q / Zhang K

History

Deposition	Sep 3, 2024	-
Header (metadata) release	Sep 10, 2025	-
Map release	Sep 10, 2025	-
Update	Sep 10, 2025	-
Current status	Sep 10, 2025	Processing site: RCSB / Status: Released

Map

• File: Download / File: emd_46847.map.gz / Format: CCP4 / Size: 216 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
• Annotation: structure of dynactin, dynein tail with one BICDR from dynein-dynactin-BICDR on microtubules
• Voxel size: X=Y=Z: 1.736 Å

Density

Contour Level	By AUTHOR: 0.1
Minimum - Maximum	-0.19845481 - 0.46096638
Average (Standard dev.)	-0.00042479584 (±0.02230078)

• Symmetry: Space group: 1

Details

EMDB XML:

Map geometry	Axis order X Y Z Origin 0 0 0 Dimensions 384 384 384 Spacing 384 384 384
Cell	A=B=C: 666.62396 Å α=β=γ: 90.0 °

Supplemental data

Half map: half

• File: emd_46847_half_map_1.map
• Annotation: half

Half map: half

• File: emd_46847_half_map_2.map
• Annotation: half

Sample components

Entire : Dynactin, dynein tail with one BICDR of dynein-dynactin-BICDR com...

• Entire: Name: Dynactin, dynein tail with one BICDR of dynein-dynactin-BICDR complex on microtubules

Components

• Complex: Dynactin, dynein tail with one BICDR of dynein-dynactin-BICDR complex on microtubules
  • Protein or peptide: Alpha-centractin
  • Protein or peptide: Actin, cytoplasmic 1
  • Protein or peptide: Actin-related protein 10
  • Protein or peptide: F-actin-capping protein subunit alpha-1
  • Protein or peptide: F-actin-capping protein subunit beta
  • Protein or peptide: Dynactin subunit 2
  • Protein or peptide: Dynactin subunit 3
  • Protein or peptide: Dynactin subunit 6
  • Protein or peptide: Dynactin subunit 5
  • Protein or peptide: Dynactin subunit 1
  • Protein or peptide: Dynactin subunit 4
  • Protein or peptide: BICD family-like cargo adapter 1
  • Protein or peptide: Cytoplasmic dynein 1 heavy chain 1
  • Protein or peptide: Cytoplasmic dynein 1 intermediate chain 2
  • Protein or peptide: Dynein light intermediate chain
• Ligand: ADENOSINE-5'-DIPHOSPHATE
• Ligand: ADENOSINE-5'-TRIPHOSPHATE
• Ligand: ZINC ION

Supramolecule #1: Dynactin, dynein tail with one BICDR of dynein-dynactin-BICDR com...

• Supramolecule: Name: Dynactin, dynein tail with one BICDR of dynein-dynactin-BICDR complex on microtubules; type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#15
• Source (natural): Organism: Sus scrofa (pig)
• Molecular weight: Theoretical: 5 MDa

Macromolecule #1: Alpha-centractin

• Macromolecule: Name: Alpha-centractin / type: protein_or_peptide / ID: 1 / Number of copies: 8 / Enantiomer: LEVO
• Source (natural): Organism: Sus scrofa (pig)
• Molecular weight: Theoretical: 42.670688 KDa

Sequence

String:

MESYDVIANQ PVVIDNGSGV IKAGFAGDQI PKYCFPNYVG RPKHVRVMAG ALEGDIFIGP KAEEHRGLLS IRYPMEHGIV KDWNDMERI WQYVYSKDQL QTFSEEHPVL LTEAPLNPRK NRERAAEVFF ETFNVPALFI SMQAVLSLYA TGRTTGVVLD S GDGVTHAV PIYEGFAMPH SIMRIDIAGR DVSRFLRLYL RKEGYDFHSS SEFEIVKAIK ERACYLSINP QKDETLETEK AQ YYLPDGS TIEIGPSRFR APELLFRPDL IGEESEGIHE VLVFAIQKSD MDLRRTLFSN IVLSGGSTLF KGFGDRLLSE VKK LAPKDV KIRISAPQER LYSTWIGGSI LASLDTFKKM WVSKKEYEED GARSIHRKTF

UniProtKB: Alpha-centractin

Macromolecule #2: Actin, cytoplasmic 1

• Macromolecule: Name: Actin, cytoplasmic 1 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
• Source (natural): Organism: Sus scrofa (pig)
• Molecular weight: Theoretical: 41.78266 KDa

Sequence

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

Macromolecule #3: Actin-related protein 10

• Macromolecule: Name: Actin-related protein 10 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
• Source (natural): Organism: Sus scrofa (pig)
• Molecular weight: Theoretical: 46.250785 KDa

Sequence

String:

MPLYEGLGSG GEKTAVVIDL GEAFTKCGFA GETGPRCIIP SVIKKAGMPK PIKVVQYNIN TEELYSYLKE FIHILYFRHL LVNPRDRRV VVIESVLCPS HFRETLTRVL FKYFEVPSVL LAPSHLMALL TLGINSAMVL DCGYRESLVL PIYEGIPVLN C WGALPLGG KALHKELETQ LLEQCTVDTG AAKEQSLPSV MGSIPEGVLE DIKVRTCFVS DLTRGLKIQA AKFNIDGNTE RP SPPPNVD YPLDGEKILH VLGSIRDSVV EILFEQDNEE KSVATLILDS LMQCPIDTRK QLAENLVIIG GTSMLPGFLH RLL AEIRYL VEKPKYKKTL GTKTFRIHTP PAKANCVAWL GGAIFGALQD ILGSRSVSKE YYNQTGRIPD WCSLNNPPLE MVFD VGKSQ PPLMKRAFST EK

UniProtKB: Actin-related protein 10

Macromolecule #4: F-actin-capping protein subunit alpha-1

• Macromolecule: Name: F-actin-capping protein subunit alpha-1 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
• Source (natural): Organism: Sus scrofa (pig)
• Molecular weight: Theoretical: 33.059848 KDa

Sequence

String:

MADFEDRVSD EEKVRIAAKF ITHAPPGEFN EVFNDVRLLL NNDNLLREGA AHAFAQYNMD QFTPVKIEGY EDQVLITEHG DLGNSRFLD PRNKISFKFD HLRKEASDPQ PEEVDGSLKS WRESCDSALR AYVKDHYSNG FCTVYAKNID GQQTIIACIE S HQFQPKNF WNGRWRSEWK FTITPPTAQV VGVLKIQVHY YEDGNVQLVS HKDVQDSVTV SNEAQTAKEF IKIIEHAENE YQ TAISENY QTMSDTTFKA LRRQLPVTRT KIDWNKILSY KIGKEMQNA

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

Macromolecule #5: F-actin-capping protein subunit beta

• Macromolecule: Name: F-actin-capping protein subunit beta / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
• Source (natural): Organism: Sus scrofa (pig)
• Molecular weight: Theoretical: 30.669768 KDa

Sequence

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

Macromolecule #6: Dynactin subunit 2

• Macromolecule: Name: Dynactin subunit 2 / type: protein_or_peptide / ID: 6 / Number of copies: 4 / Enantiomer: LEVO
• Source (natural): Organism: Sus scrofa (pig)
• Molecular weight: Theoretical: 44.704414 KDa

Sequence

String:

MADPKYADLP GIARNEPDVY ETSDLPEDDQ AEFDAELEEL TSTSVEHIIV NPNAAYDKFK DKRVGTKGLD FSDRIGKTKR TGYESGEYE MLGEGLGVKE TPQQKYQRLL HEVQELTTEV EKIKMTVKES ATEEKLTPVV LAKQLAALKQ QLVASHLEKL L GPDAAINL TDPDGALAKR LLLQLEATKN TKGAGSGGKT TSGSPPDSSL VTYELHSRPE QDKFSQAAKV AELEKRLTEL EA TVRCDQD AQNPLSAGLQ GACLMETVEL LQAKVSALDL AVLDQVEARL QSVLGKVNEI AKHKASVEDA DTQSKVHQLY ETI QRWSPI ASTLPELVQR LVTIKQLHEQ AMQFGQLLTH LDTTQQMIAC SLKDNATLLT QVQTTMRENL STVEGNFANI DERM KKLGK

UniProtKB: Dynactin subunit 2

Macromolecule #7: Dynactin subunit 3

• Macromolecule: Name: Dynactin subunit 3 / type: protein_or_peptide / ID: 7 / Number of copies: 2 / Enantiomer: LEVO
• Source (natural): Organism: Sus scrofa (pig)
• Molecular weight: Theoretical: 21.192477 KDa

Sequence

String:

MAGVTDVQRL QARLEELERW VYGPGGSRGS RKVADGLVKV QVALGNIASK RERVKILYKK IEDLIKYLDP EYMDRIAIPD ASKLQFILA EEQFILSQVA LLEQVEALVP MLDSAHIKAV PEHAARLQRL AQIHIQQQDQ CVEITEESKA LLEEYNKTTM L LSKQFVQW DELLCQLEAA KQVKPAEE

UniProtKB: Dynactin subunit 3

Macromolecule #8: Dynactin subunit 6

• Macromolecule: Name: Dynactin subunit 6 / type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
• Source (natural): Organism: Sus scrofa (pig)
• Molecular weight: Theoretical: 20.70391 KDa

Sequence

String:

MAEKTQKSVK IAPGAVVCVE SEIRGDVTIG PRTVIHPKAR IIAEAGPIVI GEGNLIEEQA LIINAHPDNI TPDAEDSEPK PMIIGTNNV FEVGCYSQAM KMGDNNVIES KAYVGRNVIL TSGCIIGACC NLNTFEVIPE NTVIYGADCL RRVQTERPQP Q TLQLDFLM KILPNYHHLK KTMKGSSTPV KN

UniProtKB: Dynactin subunit 6

Macromolecule #9: Dynactin subunit 5

• Macromolecule: Name: Dynactin subunit 5 / type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO
• Source (natural): Organism: Sus scrofa (pig)
• Molecular weight: Theoretical: 20.150533 KDa

Sequence

String:

MELGELLYNK SEYIETASGN KVSRQSVLCG SQNIVLNGKT IVMNDCIIRG DLANVRVGRH CVVKSRSVIR PPFKKFSKGV AFFPLHIGD HVFIEEDCVV NAAQIGSYVH VGKNCVIGRR CVLKDCCKIL DNTVLPPETV VPPFTVFSGC PGLFSGELPE C TQELMIDV TKSYYQKFLP LTQV

UniProtKB: Dynactin subunit 5

Macromolecule #10: Dynactin subunit 1

• Macromolecule: Name: Dynactin subunit 1 / type: protein_or_peptide / ID: 10 / Number of copies: 2 / Enantiomer: LEVO
• Source (natural): Organism: Sus scrofa (pig)
• Molecular weight: Theoretical: 142.015484 KDa

Sequence

String:

MAQSKRHVYS RTPSGSRMSA EASARPLRVG SRVEVIGKGH RGTVAYVGAT LFATGKWVGV ILDEAKGKND GTVQGRKYFT CDEGHGIFV RQSQIQVFED GADTTSPETP DSSASKVLRR EGTDSNAKTS KLRGPKPKKA PTARKTTTRR PKPTRPASTG V AGASSSLG PSGSASAGEL SSSEPSTPAQ TPLAAPIIPT PALTSPGAAP PLPSPSKEEE GLRAQVRDLE EKLETLRLKR AE DKAKLKE LEKHKIQLEQ VQEWKSKMQE QQADLQRRLK EARKEAKEAL EAKERYMEEM ADTADAIEMA TLDKEMAEER AES LQQEVE ALKERVDELT TDLEILKAEI EEKGSDGAAS SYQLKQLEEQ NARLKDALVR MRDLSSSEKQ EHVKLQKLME KKNQ ELEVV RQQRERLQEE LSQAESTIDE LKEQVDAALG AEEMVEMLTD RNLNLEEKVR ELRETVGDLE AMNEMNDELQ ENARE TELE LREQLDMAGA RVREAQKRVE AAQETVADYQ QTIKKYRQLT AHLQDVNREL TNQQEASVER QQQPPPETFD FKIKFA ETK AHAKAIEMEL RQMEVAQANR HMSLLTAFMP DSFLRPGGDH DCVLVLLLMP RLICKAELIR KQAQEKFDLS ENCSERP GL RGAAGEQLSF AAGLVYSLSL LQATLHRYEH ALSQCSVDVY KKVGSLYPEM SAHERSLDFL IELLHKDQLD ETVNVEPL T KAIKYYQHLY SIHLAEQPED STMQLADHIK FTQSALDCMS VEVGRLRAFL QGGQEASDIA LLLRDLETSC SDIRQFCKK IRRRMPGTDA PGIPAALAFG AQVSDTLLDC RKHLTWVVAV LQEVAAAAAQ LIAPLAENEG LPVAALEELA FKASEQIYGT PSSSPYECL RQSCNILIST MNKLATAMQE GEYDAERPPS KPPPVELRAA ALRAEITDAE GLGLKLEDRE TVIKELKKSL K IKGEELSE ANVRLSLLEK KLDSAAKDAD ERIEKVQTRL EETQALLRKK EKEFEETMDA LQADIDQLEA EKAELKQRLN SQ SKRTIEG IRGPPPSGIA TLVSGIAGEE QQRGGAPGQA PGIVPGPGLV KDSPLLLQQI SAMRLHISQL QHENSVLKGA QMK ASLAAL PPLHVAKLSL PPHEGPGSEL AAGALYRKTN QLLETLNQLS THTHVVDITR SSPAAKSPSA QLLEQVTQLK SLSD TIEKL KDEVLKETVS QRPGATVPTD FATFPSSAFL RAKEEQQDDT VYMGKVTFSC AAGLGQRHRL VLTQEQLHQL HDRLI S

UniProtKB: Dynactin subunit 1

Macromolecule #11: Dynactin subunit 4

• Macromolecule: Name: Dynactin subunit 4 / type: protein_or_peptide / ID: 11 / Number of copies: 1 / Enantiomer: LEVO
• Source (natural): Organism: Sus scrofa (pig)
• Molecular weight: Theoretical: 52.920434 KDa

Sequence

String:

MASLLQSERV LYLVQGEKKV RAPLSQLYFC RYCSELRSLE CVSHEVDSHY CPSCLENMPS AEAKLKKNRC ANCFDCPGCM HTLSTRATS ISTQLPDDPA KTAVKKAYYL ACGFCRWTSR DVGMADKSVA SGGWQEPDHP HTQRMNKLIE YYQQLAQKEK V ERDRKKLA RRRNYMPLAF SQHTIHVVDK YGLGTRLQRP RAGTTITALA GLSLKEGEDQ KEIKIEPAQA VDEVEPLPED YY TRPVNLT EVTTLQQRLL QPDFQPICAS QLYPRHKHLL IKRSLRCRQC EHNLSKPEFN PTSIKFKIQL VAVNYIPEVR IMS IPNLRY MKESQVLLTL TNPVENLTHV TLLECEEGDP DDTNSTAKVS VPPTELVLAG KDAAAEYDEL AEPQDFPDDP DVVA FRKAN KVGVFIKVTP QREEGDVTVC FKLKHDFKNL AAPIRPVEEA DPGAEVSWLT QHVELSLGPL LP

UniProtKB: Dynactin subunit 4

Macromolecule #12: BICD family-like cargo adapter 1

• Macromolecule: Name: BICD family-like cargo adapter 1 / type: protein_or_peptide / ID: 12 / Number of copies: 2 / Enantiomer: LEVO
• Source (natural): Organism: Mus musculus (house mouse)
• Molecular weight: Theoretical: 65.377035 KDa
• Recombinant expression: Organism: Spodoptera frugiperda (fall armyworm)

Sequence

String:

MSAFCLGLAG RASAPAEPDS ACCMELPAGA GDAVRSPATA AALVSFPGGP GELELALEEE LALLAAGERS SEPGEHPQAE PESPVEGHG PPLPPPPTQD PELLSVIRQK EKDLVLAARL GKALLERNQD MSRQYEQMHK ELTDKLEHLE QEKHELRRRF E NREGEWEG RVSELETDVK QLQDELERQQ LHLREADREK TRAVQELSEQ NQRLLDQLSR ASEVERQLSM QVHALKEDFR EK NSSTNQH IIRLESLQAE IKMLSDRKRE LEHRLSATLE ENDLLQGTVE ELQDRVLILE RQGHDKDLQL HQSQLELQEV RLS YRQLQG KVEELTEERS LQSSAATSTS LLSEIEQSME AEELEQEREQ LRLQLWEAYC QVRYLCSHLR GNDSADSAVS TDSS MDESS ETSSAKDVPA GSLRTALNDL KRLIQSIVDG VEPTVTLLSV EMTALKEERD RLRVTSEDKE PKEQLQKAIR DRDEA IAKK NAVELELAKC KMDMMSLNSQ LLDAIQQKLN LSQQLEAWQD DMHRVIDRQL MDTHLKEQSR PAAAAFPRGH GVGRGQ EPS TADGKRLFSF FRKI

UniProtKB: BICD family-like cargo adapter 1

Macromolecule #13: Cytoplasmic dynein 1 heavy chain 1

• Macromolecule: Name: Cytoplasmic dynein 1 heavy chain 1 / type: protein_or_peptide / ID: 13 / Number of copies: 4 / Enantiomer: LEVO
• Source (natural): Organism: Sus scrofa (pig)
• Molecular weight: Theoretical: 532.739562 KDa

Sequence

String:

MSEPGGGGGE DGSAGLEVSA VQNVADVSVL QKHLRKLVPL LLEDGGEAPA ALEAALEEKS ALEQMRKFLS DPQVHTVLVE RSTLKEDVG DEGEEEKEFI SYNINIDIHY GVKSNSLAFI KRAPVIDADK PVSSQLRVLT LSEDSPYETL HSFISNAVAP F FKSYIRES GKADRDGDKM APSVEKKIAE LEMGLLHLQQ NIEIPEISLP IHPIITNVAK QCYERGEKPK VTDFGDKVED PT FLNQLQS GVNRWIREIQ KVTKLDRDPA SGTALQEISF WLNLERALYR IQEKRESPEV LLTLDILKHG KRFHATVSFD TDT GLKQAL ETVNDYNPLM KDFPLNDLLS ATELDKIRQA LVAIFTHLRK IRNTKYPIQR ALRLVEAISR DLSSQLLKVL GTRK LMHVA YEEFEKVMVA CFEVFQTWDD EYEKLQVLLR DIVKRKREEN LKMVWRINPA HRKLQARLDQ MRKFRRQHEQ LRAVI VRVL RPQVTAVAQQ NQGEAPEPQD MKVAEVLFDA ADANAIEEVN LAYENVKEVD GLDVSKEGTE AWEAAMKRYD ERIDRV ETR ITARLRDQLG TAKNANEMFR IFSRFNALFV RPHIRGAIRE YQTQLIQRVK DDIESLHDKF KVQYPQSQAC KMSHVRD LP PVSGSIIWAK QIDRQLTAYM KRVEDVLGKG WENHVEGQKL KQDGDSFRMK LNTQEIFDDW ARKVQQRNLG VSGRIFAI E STRVRGRSGN VLKLKVNFLP EIITLSKEVR NLKWLGFRVP LAIVNKAHQA NQLYPFAISL IESVRTYERT CEKVEERNT ISLLVAGLKK EVQALIAEGI ALVWESYKLD PYVQRLAETV FNFQEKVDDL LIIEEKIDLE VRSLETCVYD HKTFSEILNR VQKAVDDLN LHSYSNLPIW VNKLDMEIER ILGVRLQAGL RAWTQVLLGQ AEDKAEVDMD TDAPQVSHKP GGEPKIKNVV H ELRITNQV IYLNPPIEEC RYKLYQEMFA WKMVVLSLPR IQSQRYQVGV HYELTEEEKF YRNALTRMPD GPVALEESYS AV MGIVTEV EQYVKVWLQY QCLWDMQAEN IYNRLGEDLN KWQALLVQIR KARGTFDNAE TKKEFGPVVI DYGKVQSKVN LKY DSWHKE VLSKFGQMLG SNMTEFHSQI SKSRQELEQH SVDTASTSDA VTFITYVQSL KRKIKQFEKQ VELYRNGQRL LEKQ RFQFP PSWLYIDNIE GEWGAFNDIM RRKDSAIQQQ VANLQMKIVQ EDRAVESRTT DLLADWEKTK PVTGNLRPEE ALQAL TIYE GKFGRLKDDR EKCAKAKEAL ELTETGLLSG SEERVQVALE ELQDLKGVWS ELSKIWEQID QMKEQPWVSV QPRKLR QNL DGLLNQLKNF PARLRQYASY EFVQRLLKGY LKINMLVIEL KSEALKDRHW KQLMKRLHVN WVVSELTLGQ IWDVDLQ KN EAVVKDVLLV AQGEMALEEF LKQIREVWNT YELDLVNYQN KCRLIRGWDD LFNKVKEHIN SVSAMKLSPY YKVFEEDA L SWEDKLNRIM ALFDVWIDVQ RRWVYLEGIF TGSADIKHLL PVETQRFQSI STEFLALMKK VSKSPLVMDV LNIQGVQRS LERLADLLGK IQKALGEYLE RERSSFPRFY FVGDEDLLEI IGNSKNVAKL QKHFKKMFAG VSSIILSEDN SVVLGISSRE GEEVTFKTP VSITEHPKIN EWLTLVEKEM RVTLAKLLAE SVTEVEIFGK ATSIDPNTYI TWIDKYQAQL VVLSAQIAWS E NVEAALSS IGGSGDSAPL QSVLSNVEVT LNVLADSVLM EQPPLRRRKL EHLITELVHQ RDVTRSLIKS KIDNAKSFEW LS QMRFYFD PKQTDVLQQL SIQMANAKFN YGFEYLGVQD KLVQTPLTDR CYLTMTQALE ARLGGSPFGP AGTGKTESVK ALG HQLGRF VLVFNCDETF DFQAMGRIFV GLCQVGAWGC FDEFNRLEER MLSAVSQQVQ CIQEALREHS SPNHDKASAP ITCE LLNKQ VKVSPDMAIF ITMNPGYAGR SNLPDNLKKL FRSLAMTKPD RQLIAQVMLY SQGFRTAEVL ANKIVPFFKL CDEQL SSQS HYDFGLRALK SVLVSAGNVK RERIQKIKRE KEERGEAVDE GEIAENLPEQ EILIQSVCET MVPKLVAEDI PLLFSL LSD VFPGVQYHRG EMTALREELK KVCQEMYLTY GDGEEVGGMW VEKVLQLYQI TQINHGLMMV GPSGSGKSMA WRVLLKA LE RLEGVEGVAH IIDPKAISKD HLYGTLDPNT REWTDGLFTH VLRKIIDNVR GELQKRQWIV FDGDVDPEWV ENLNSVLD D NKLLTLPNGE RLSLPPNVRI MFEVQDLKYA TLATVSRCGM VWFSEDVLST DMIFNNFLAR LRSIPLDEGE DEAQRRRKG KEDEGEEAAS PMLQIQRDAA TTLQPYFTPN GLVTKALEHA FKLEHIMDLT RLRCLGSLFS MLHQACRNVA QYNANHPDFP MQMEQLERY IQRYLVYAIL WSLSGDSRLK MRAELGEYIR RITTVPLPAA PNIPIIDYEV SISGEWSPWQ AKVPQIEVET H KVAAPDVV VPTLDTVRHE ALLYTWLAEH KPLVLCGPPG SGKTMTLFSA LRALPDMEVV GLNFSSATTP ELLLKTFDHY CE YRRTPNG VVLAPVQLGK WLVLFCDEIN LPDMDKYGTQ RVISFIRQMV EHGGFYRTSD QTWVKLERIQ FVGACNPPTD PGR KPLSHR FLRHVPVVYV DYPGPASLTQ IYGTFNRAML RLVPSLRTYA EPLTAAMVEF YTMSQERFTQ DTQPHYIYSP REMT RWVRG IFEALRPLET LPVEGLIRIW AHEALRLFQD RLVEDEERRW TDENIDLVAL KHFPNIDKEK AMSRPILYSN WLSKD YIPV DQEELRDYVK ARLKVFYEEE LDVPLVLFNE VLDHVLRIDR IFRQPQGHLL LIGVSGAGKT TLSRFVAWMN GLSVYQ IKV HRKYTGEDFD EDLRTVLRRS GCKNEKIAFI MDESNVLDSG FLERMNTLLA NGEVPGLFEG DEYATLMTQC KEGAQKE GL MLDSHEELYK WFTSQVIRNL HVVFTMNPSS EGLKDRAATS PALFNRCVLN WFGDWSTEAL YQVGKEFTSK MDLEKPNY V VPDYMPVVYD KLPQPPSHRE AIVNSCVFVH QTLHQANARL AKRGGRTMAI TPRHYLDFIN HYANLFHEKR SELEEQQMH LNVGLRKIKE TVDQVEELRR DLRIKSQELE VKNAAANDKL KKMVKDQQEA EKKKVMSQEI QEQLHKQQEV IADKQMSVKE DLDKVEPAV IEAQNAVKSI KKQHLVEVRS MANPPAAVKL ALESICLLLG ESTTDWKQIR SIIMRENFIP TIVNFSAEEI S DAIREKMK KNYMSNPSYN YEIVNRASLA CGPMVKWAIA QLNYADMLKR VEPLRNELQK LEDDAKDNQQ KANEVEQMIR DL EASIARY KEEYAVLISE AQAIKADLAA VEAKVNRSTA LLKSLSAERE RWEKTSETFK NQMSTIAGDC LLSAAFIAYA GYF DQQMRQ NLFTTWSHHL QQANIQFRTD IARTEYLSNA DERLRWQASS LPADDLCTEN AIMLKRFNRY PLIIDPSGQA TEFI MNEYK DRKITRTSFL DDAFRKNLES ALRFGNPLLV QDVESYDPVL NPVLNREVRR TGGRVLITLG DQDIDLSPSF VIFLS TRDP TVEFPPDLCS RVTFVNFTVT RSSLQSQCLN EVLKAERPDV DEKRSDLLKL QGEFQLRLRQ LEKSLLQALN EVKGRI LDD DTIITTLENL KREAAEVTRK VEETDIVMQE VETVSQQYLP LSTACSSIYF TMESLKQIHF LYQYSLQFFL DIYHNVL YE NPNLKGVTDH TQRLCIITKD LFQVAFNRVA RGMLHQDHIT FAMLLARIKL KGTVGEPTYE AEFQHFLRGK EIVLSAGS T PKIPGLTVEQ AEAVVRLSCL PAFKDLIAKV QADEQFSIWL DSSSPEQTVP HLWSEENPAT PIGQAIHRLL LIQAFRPDR LLAMAHVFVS TNLGESFMSI MEQPLDLTHI VDTEVKPNTP VLMCSVPGYD ASGHVEDLAA EQNTQITSIA IGSAEGFNQA DKAINTAVK SGRWVMLKNV HLAPGWLMQL EKKLHSLQPH ACFRLFLTME INPKVPVNLL RAGRIFVFEP PPGVKANMLR T FSSVPVSR ICKSPNERAR LYFLLAWFHA IIQERLRYAP LGWSKKYEFG ESDLRSACDT VDTWLDDTAK GRQNISPDKI PW SALKTLM AQSIYGGRVD NEFDQRLLNT FLERLFTTRS FDSEFKLACK VDGHKDIQMP DGIRREEFVQ WVELLPDTQT PSW LGLPNN AERVLLTTQG VDMISKMLKM QMLEDEDDLA YAETEKKTRT DSTADGRPAW MRTLHTTASN WLHLIPQTLS HLKR TVDNI KDPLFRFFER EVKMGARLLQ DVRQDLADVV QVCEGKKKQT NYLRTLINEL VKGILPRSWS HYTVPAGMTV IQWVS DFSE RIKQLQSVSQ AAASGGAKEL KNIHVCLGGL FVPEAYITAT RQYVAQANSW SLEELCLEVI VTTSQSATLD ACSFGV TGL KLQGATCSNN KLSLSNAIST VLPLTQLRWV KQTNAEKKAN VVTLPVYLNF TRADLIFTVD FEIATKEDPR SFYERGV AV LCTE

UniProtKB: Cytoplasmic dynein 1 heavy chain 1

Macromolecule #14: Cytoplasmic dynein 1 intermediate chain 2

• Macromolecule: Name: Cytoplasmic dynein 1 intermediate chain 2 / type: protein_or_peptide / ID: 14 / Number of copies: 4 / Enantiomer: LEVO
• Source (natural): Organism: Sus scrofa (pig)
• Molecular weight: Theoretical: 68.567219 KDa

Sequence

String:

MSDKSELKAE LERKKQRLAQ IREEKKRKEE ERKKKETDQK KEAVTSVQEE SDLEKKRREA EALLQSMGLT PESPIVPPPM SPSSKSVST PSEAGSQDSG DGAVGSRRGP IKLGMAKITQ VDFPPREIVT YTKETQTPVM AQPKEDEEEE DDVVTPKPPI E PEEEKTLK KDEESDSKAP PHELTEEEKQ QILHSEEFLS FFDHSTRIVE RALSEQINIF FDYSGRDLED KEGEIQAGAK LS LNRQFFD ERWSKHRVVS CLDWSSQYPE LLVASYNNNE DAPHEPDGVA LVWNMKYKKT TPEYVFHCQS AVMSATFAKF HPN LVVGGT YSGQIVLWDN RSNKRTPVQR TPLSAAAHTH PVYCVNVVGT QNAHNLISIS TDGKICSWSL DMLSHPQDSM ELVH KQSKA VAVTSMSFPV GDVNNFVVGS EEGSVYTACR HGSKAGISEM FEGHQGPITG IHCHAAVGAV DFSHLFVTSS FDWTV KLWT TKNNKPLYSF EDNSDYVYDV MWSPTHPALF ACVDGMGRLD LWNLNNDTEV PTASISVEGN PALNRVRWTH SGREIA VGD SEGQIVIYDV GEQIAVPRND EWARFGRTLA EINANRADAE EEAATRIPA

UniProtKB: Cytoplasmic dynein 1 intermediate chain 2

Macromolecule #15: Dynein light intermediate chain

• Macromolecule: Name: Dynein light intermediate chain / type: protein_or_peptide / ID: 15 / Number of copies: 2 / Enantiomer: LEVO
• Source (natural): Organism: Sus scrofa (pig)
• Molecular weight: Theoretical: 54.227156 KDa

Sequence

String:

MAPVGVEKKL LLGPNGPAVA AAGDLTSEEE EGQSLWSSIL SEVSTRARSK LPSGKNILVF GEDGSGKTTL MTKLQGAEHG KKGRGLEYL YLSIHDEDRD DHTRCNVWIL DGDLYHKGLL KFAVSAESLP ETLVIFVADM SRPWTVMESL QKWASVLREH I DKMKIPPE EMRELERKFM KDFQDYIEPE EGSQGSPQRR GPLTSGPDEE NVALPLGDNV LTHNLGVPVL VVCTKCDAVS VL EKEHDYR DEHFDFIQSH LRRFCLQYGA ALIYTSVKEE KNLDLLYKYI VHKTYGFHFT TPALVVEKEA VFIPAGWDNE KKI AILHEN FTTVKPEDAY EDFIVKPPVR KLVHDKELAA EDEQVFLMKQ QSLLAKQPAT PTRASESPAR GPSGSPRTQG RGGP ASVPS ASPGTSVKKP DPNIKNNAAS EGVLASFFNS LLSKKTGSPG SPGAGGVQST AKKSGQKTVL TNVQEELDRM TRKPD SMVT NSSTENEA

UniProtKB: Dynein light intermediate chain

Macromolecule #16: ADENOSINE-5'-DIPHOSPHATE

• Macromolecule: Name: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 16 / Number of copies: 9 / Formula: ADP
• Molecular weight: Theoretical: 427.201 Da

Chemical component information

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

Macromolecule #17: ADENOSINE-5'-TRIPHOSPHATE

• Macromolecule: Name: ADENOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 17 / Number of copies: 1 / Formula: ATP
• Molecular weight: Theoretical: 507.181 Da

Chemical component information

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

Macromolecule #18: ZINC ION

• Macromolecule: Name: ZINC ION / type: ligand / ID: 18 / Number of copies: 3 / Formula: ZN
• Molecular weight: Theoretical: 65.409 Da

Experimental details

Structure determination

• Method: cryo EM
• Processing: single particle reconstruction
• Aggregation state: particle

Sample preparation

• Buffer: pH: 7.2
• Vitrification: Cryogen name: ETHANE

Electron microscopy

• Microscope: TFS GLACIOS
• Image recording: Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 40.0 e/Ų
• Electron beam: Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN
• Electron optics: Calibrated defocus max: 3.0 µm / Calibrated defocus min: 1.2 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.2 µm

Image processing

• CTF correction: Type: PHASE FLIPPING AND AMPLITUDE CORRECTION
• Startup model: Type of model: NONE
• Final reconstruction: Resolution.type: BY AUTHOR / Resolution: 7.2 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 10750
• Initial angle assignment: Type: MAXIMUM LIKELIHOOD
• Final angle assignment: Type: MAXIMUM LIKELIHOOD