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- EMDB-44306: Cryo-EM structure of human dynactin complex bound to Chlamydia ef... -

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Basic information

Entry
Database: EMDB / ID: EMD-44306
TitleCryo-EM structure of human dynactin complex bound to Chlamydia effector Dre1
Map data
Sample
  • Complex: Human dynactin complex bound to Chlamydia effector Dre1
    • Protein or peptide: x 14 types
  • Ligand: x 3 types
KeywordsHuman dynactin / Chlamydia effector / host-pathogen interaction / MOTOR PROTEIN
Function / homology
Function and homology information


retrograde axonal transport of mitochondrion / cell cortex region / centriolar subdistal appendage / positive regulation of neuromuscular junction development / dynactin complex / centriole-centriole cohesion / microtubule anchoring at centrosome / F-actin capping protein complex / WASH complex / sperm head-tail coupling apparatus ...retrograde axonal transport of mitochondrion / cell cortex region / centriolar subdistal appendage / positive regulation of neuromuscular junction development / dynactin complex / centriole-centriole cohesion / microtubule anchoring at centrosome / F-actin capping protein complex / WASH complex / sperm head-tail coupling apparatus / maintenance of synapse structure / ventral spinal cord development / positive regulation of norepinephrine uptake / melanosome transport / cellular response to cytochalasin B / cytoskeleton-dependent cytokinesis / nuclear membrane disassembly / bBAF complex / microtubule plus-end / npBAF complex / regulation of transepithelial transport / nBAF complex / brahma complex / morphogenesis of a polarized epithelium / XBP1(S) activates chaperone genes / positive regulation of microtubule nucleation / protein localization to adherens junction / postsynaptic actin cytoskeleton / structural constituent of postsynaptic actin cytoskeleton / Formation of the dystrophin-glycoprotein complex (DGC) / GBAF complex / Formation of annular gap junctions / Tat protein binding / regulation of G0 to G1 transition / Gap junction degradation / Folding of actin by CCT/TriC / Cell-extracellular matrix interactions / dense body / barbed-end actin filament capping / cell junction assembly / actin polymerization or depolymerization / regulation of nucleotide-excision repair / non-motile cilium assembly / regulation of double-strand break repair / coronary vasculature development / Prefoldin mediated transfer of substrate to CCT/TriC / RSC-type complex / apical protein localization / adherens junction assembly / dynein complex / RHOD GTPase cycle / regulation of cell morphogenesis / RHOF GTPase cycle / Adherens junctions interactions / retrograde transport, endosome to Golgi / COPI-independent Golgi-to-ER retrograde traffic / tight junction / protein localization to centrosome / Sensory processing of sound by outer hair cells of the cochlea / Interaction between L1 and Ankyrins / SWI/SNF complex / regulation of mitotic metaphase/anaphase transition / cytoplasmic dynein complex / microtubule associated complex / Sensory processing of sound by inner hair cells of the cochlea / lamellipodium assembly / aorta development / ventricular septum development / positive regulation of T cell differentiation / motor behavior / regulation of norepinephrine uptake / nuclear migration / transporter regulator activity / apical junction complex / nitric-oxide synthase binding / neuromuscular process / mitotic metaphase chromosome alignment / positive regulation of double-strand break repair / neuromuscular junction development / spectrin binding / maintenance of blood-brain barrier / NuA4 histone acetyltransferase complex / establishment or maintenance of cell polarity / cortical cytoskeleton / dynein complex binding / positive regulation of stem cell population maintenance / cell leading edge / Regulation of MITF-M-dependent genes involved in pigmentation / regulation of synaptic vesicle endocytosis / Recycling pathway of L1 / regulation of G1/S transition of mitotic cell cycle / establishment of mitotic spindle orientation / brush border / cleavage furrow / kinesin binding / Advanced glycosylation endproduct receptor signaling / negative regulation of cell differentiation / EPH-ephrin mediated repulsion of cells / RHO GTPases Activate WASPs and WAVEs / positive regulation of myoblast differentiation
Similarity search - Function
Dynactin subunit 3 / Dynactin subunit p22 / Dynactin subunit 4 / Dynactin p62 family / Dynein associated protein / Dynein associated protein / Dynamitin / : / Dynamitin / Dynactin subunit 6 ...Dynactin subunit 3 / Dynactin subunit p22 / Dynactin subunit 4 / Dynactin p62 family / Dynein associated protein / Dynein associated protein / Dynamitin / : / Dynamitin / Dynactin subunit 6 / Dynactin subunit 5 / 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 / 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
Similarity search - Domain/homology
Dynactin subunit 6 / Dynactin subunit 3 / F-actin-capping protein subunit beta / F-actin-capping protein subunit alpha-1 / Actin, cytoplasmic 1 / Alpha-centractin / Dynactin subunit 2 / Dynactin subunit 1 / Dynactin subunit 5 / Actin-related protein 10 / Dynactin subunit 4
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.49 Å
AuthorsPawar KI / Verba KA
Funding support1 items
OrganizationGrant numberCountry
Not funded
CitationJournal: Cell Rep / Year: 2025
Title: The Chlamydia effector Dre1 binds dynactin to reposition host organelles during infection.
Authors: Jessica Sherry / Komal Ishwar Pawar / Lee Dolat / Erin Smith / I-Chang Chang / Khavong Pha / Robyn Kaake / Danielle L Swaney / Clara Herrera / Eleanor McMahon / Robert J Bastidas / Jeffrey R ...Authors: Jessica Sherry / Komal Ishwar Pawar / Lee Dolat / Erin Smith / I-Chang Chang / Khavong Pha / Robyn Kaake / Danielle L Swaney / Clara Herrera / Eleanor McMahon / Robert J Bastidas / Jeffrey R Johnson / Raphael H Valdivia / Nevan J Krogan / Cherilyn A Elwell / Kliment Verba / Joanne N Engel /
Abstract: The obligate intracellular pathogen Chlamydia trachomatis replicates in a specialized membrane-bound compartment where it repositions host organelles during infection to acquire nutrients and evade ...The obligate intracellular pathogen Chlamydia trachomatis replicates in a specialized membrane-bound compartment where it repositions host organelles during infection to acquire nutrients and evade host surveillance. We describe a bacterial effector, Dre1, that binds specifically to dynactin associated with host microtubule organizing centers without globally impeding dynactin function. Dre1 is required to reposition the centrosome, mitotic spindle, Golgi apparatus, and primary cilia around the inclusion and contributes to pathogen fitness in cell-based and mouse models of infection. We utilized Dre1 to affinity purify the megadalton dynactin protein complex and determined the first cryoelectron microscopy (cryo-EM) structure of human dynactin. Our results suggest that Dre1 binds to the pointed end of dynactin and uncovers the first bacterial effector that modulates dynactin function. Our work highlights how a pathogen employs a single effector to evoke targeted, large-scale changes in host cell organization that facilitate pathogen growth without inhibiting host viability.
History
DepositionMar 27, 2024-
Header (metadata) releaseApr 16, 2025-
Map releaseApr 16, 2025-
UpdateApr 16, 2025-
Current statusApr 16, 2025Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_44306.png

Downloads & links

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Map

FileDownload / File: emd_44306.map.gz / Format: CCP4 / Size: 2.4 GB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
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Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.84 Å/pix.
x 864 pix.
= 721.44 Å		0.84 Å/pix.
x 864 pix.
= 721.44 Å		0.84 Å/pix.
x 864 pix.
= 721.44 Å

Surface

Projections

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Images are generated by Spider.

Voxel sizeX=Y=Z: 0.835 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 6.0
Minimum - Maximum-14.4564705 - 30.993486000000001
Average (Standard dev.)-0.0071130265 (±1.5730469)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions864864864
Spacing864864864
CellA=B=C: 721.44 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #1

Fileemd_44306_half_map_1.map
Projections & Slices
AxesZYX

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Slices (1/2)
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Histogram (log scale)

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Half map: #2

Fileemd_44306_half_map_2.map
Projections & Slices
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Sample components

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Entire : Human dynactin complex bound to Chlamydia effector Dre1

EntireName: Human dynactin complex bound to Chlamydia effector Dre1
Components
  • Complex: Human dynactin complex bound to Chlamydia effector Dre1
    • Protein or peptide: Alpha-centractin
    • Protein or peptide: Actin, cytoplasmic 1
    • Protein or peptide: Actin-related protein 10
    • Protein or peptide: Dynactin subunit 4
    • Protein or peptide: Dynactin subunit 5
    • Protein or peptide: Dynactin subunit 6
    • 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 1
    • Protein or peptide: Dynactin subunit 1, p150-glued
    • Protein or peptide: Dynactin subunit 2, p50 dynamitin
    • Protein or peptide: Dynactin subunit 1
  • Ligand: ADENOSINE-5'-DIPHOSPHATE
  • Ligand: PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
  • Ligand: ZINC ION

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Supramolecule #1: Human dynactin complex bound to Chlamydia effector Dre1

SupramoleculeName: Human dynactin complex bound to Chlamydia effector Dre1
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#14
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 1.1 MDa

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Macromolecule #1: Alpha-centractin

MacromoleculeName: Alpha-centractin / type: protein_or_peptide / ID: 1 / Number of copies: 8 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 42.670688 KDa
SequenceString: MESYDVIANQ PVVIDNGSGV IKAGFAGDQI PKYCFPNYVG RPKHVRVMAG ALEGDIFIGP KAEEHRGLLS IRYPMEHGIV KDWNDMERI WQYVYSKDQL QTFSEEHPVL LTEAPLNPRK NRERAAEVFF ETFNVPALFI SMQAVLSLYA TGRTTGVVLD S GDGVTHAV ...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

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Macromolecule #2: Actin, cytoplasmic 1

MacromoleculeName: Actin, cytoplasmic 1 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
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 #3: Actin-related protein 10

MacromoleculeName: Actin-related protein 10 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 46.360863 KDa
SequenceString: MPLYEGLGSG GEKTAVVIDL GEAFTKCGFA GETGPRCIIP SVIKRAGMPK PVRVVQYNIN TEELYSYLKE FIHILYFRHL LVNPRDRRV VIIESVLCPS HFRETLTRVL FKYFEVPSVL LAPSHLMALL TLGINSAMVL DCGYRESLVL PIYEGIPVLN C WGALPLGG ...String:
MPLYEGLGSG GEKTAVVIDL GEAFTKCGFA GETGPRCIIP SVIKRAGMPK PVRVVQYNIN TEELYSYLKE FIHILYFRHL LVNPRDRRV VIIESVLCPS HFRETLTRVL FKYFEVPSVL LAPSHLMALL TLGINSAMVL DCGYRESLVL PIYEGIPVLN C WGALPLGG KALHKELETQ LLEQCTVDTS VAKEQSLPSV MGSVPEGVLE DIKARTCFVS DLKRGLKIQA AKFNIDGNNE RP SPPPNVD YPLDGEKILH ILGSIRDSVV EILFEQDNEE QSVATLILDS LIQCPIDTRK QLAENLVVIG GTSMLPGFLH RLL AEIRYL VEKPKYKKAL GTKTFRIHTP PAKANCVAWL GGAIFGALQD ILGSRSVSKE YYNQTGRIPD WCSLNNPPLE MMFD VGKTQ PPLMKRAFST EK

UniProtKB: Actin-related protein 10

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Macromolecule #4: Dynactin subunit 4

MacromoleculeName: Dynactin subunit 4 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 52.409016 KDa
SequenceString: MASLLQSDRV LYLVQGEKKV RAPLSQLYFC RYCSELRSLE CVSHEVDSHY CPSCLENMPS AEAKLKKNRC ANCFDCPGCM HTLSTRATS ISTQLPDDPA KTTMKKAYYL ACGFCRWTSR DVGMADKSVA SGGWQEPENP HTQRMNKLIE YYQQLAQKEK V ERDRKKLA ...String:
MASLLQSDRV LYLVQGEKKV RAPLSQLYFC RYCSELRSLE CVSHEVDSHY CPSCLENMPS AEAKLKKNRC ANCFDCPGCM HTLSTRATS ISTQLPDDPA KTTMKKAYYL ACGFCRWTSR DVGMADKSVA SGGWQEPENP HTQRMNKLIE YYQQLAQKEK V ERDRKKLA RRRNYMPLAF SDKYGLGTRL QRPRAGASIS TLAGLSLKEG EDQKEIKIEP AQAVDEVEPL PEDYYTRPVN LT EVTTLQQ RLLQPDFQPV CASQLYPRHK HLLIKRSLRC RKCEHNLSKP EFNPTSIKFK IQLVAVNYIP EVRIMSIPNL RYM KESQVL LTLTNPVENL THVTLFECEE GDPDDINSTA KVVVPPKELV LAGKDAAAEY DELAEPQDFQ DDPDIIAFRK ANKV GIFIK VTPQREEGEV TVCFKMKHDF KNLAAPIRPI EESDQGTEVI WLTQHVELSL GPLLP

UniProtKB: Dynactin subunit 4

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Macromolecule #5: Dynactin subunit 5

MacromoleculeName: Dynactin subunit 5 / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 20.150533 KDa
SequenceString:
MELGELLYNK SEYIETASGN KVSRQSVLCG SQNIVLNGKT IVMNDCIIRG DLANVRVGRH CVVKSRSVIR PPFKKFSKGV AFFPLHIGD HVFIEEDCVV NAAQIGSYVH VGKNCVIGRR CVLKDCCKIL DNTVLPPETV VPPFTVFSGC PGLFSGELPE C TQELMIDV TKSYYQKFLP LTQV

UniProtKB: Dynactin subunit 5

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Macromolecule #6: Dynactin subunit 6

MacromoleculeName: Dynactin subunit 6 / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 20.769002 KDa
SequenceString:
MAEKTQKSVK IAPGAVVCVE SEIRGDVTIG PRTVIHPKAR IIAEAGPIVI GEGNLIEEQA LIINAYPDNI TPDTEDPEPK PMIIGTNNV FEVGCYSQAM KMGDNNVIES KAYVGRNVIL TSGCIIGACC NLNTFEVIPE NTVIYGADCL RRVQTERPQP Q TLQLDFLM KILPNYHHLK KTMKGSSTPV KN

UniProtKB: Dynactin subunit 6

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Macromolecule #7: F-actin-capping protein subunit alpha-1

MacromoleculeName: F-actin-capping protein subunit alpha-1 / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 32.964727 KDa
SequenceString: MADFDDRVSD EEKVRIAAKF ITHAPPGEFN EVFNDVRLLL NNDNLLREGA AHAFAQYNMD QFTPVKIEGY EDQVLITEHG DLGNSRFLD PRNKISFKFD HLRKEASDPQ PEEADGGLKS WRESCDSALR AYVKDHYSNG FCTVYAKTID GQQTIIACIE S HQFQPKNF ...String:
MADFDDRVSD EEKVRIAAKF ITHAPPGEFN EVFNDVRLLL NNDNLLREGA AHAFAQYNMD QFTPVKIEGY EDQVLITEHG DLGNSRFLD PRNKISFKFD HLRKEASDPQ PEEADGGLKS WRESCDSALR AYVKDHYSNG FCTVYAKTID GQQTIIACIE S HQFQPKNF WNGRWRSEWK FTITPPTAQV VGVLKIQVHY YEDGNVQLVS HKDVQDSLTV SNEAQTAKEF IKIIENAENE YQ TAISENY QTMSDTTFKA LRRQLPVTRT KIDWNKILSY KIGKEMQNA

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

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Macromolecule #8: F-actin-capping protein subunit beta

MacromoleculeName: F-actin-capping protein subunit beta / type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 30.669768 KDa
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 #9: Dynactin subunit 2

MacromoleculeName: Dynactin subunit 2 / type: protein_or_peptide / ID: 9 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 44.285891 KDa
SequenceString: MADPKYADLP GIARNEPDVY ETSDLPEDDQ AEFDAEELTS TSVEHIIVNP NAAYDKFKDK RVGTKGLDFS DRIGKTKRTG YESGEYEML GEGLGVKETP QQKYQRLLHE VQELTTEVEK IKTTVKESAT EEKLTPVLLA KQLAALKQQL VASHLEKLLG P DAAINLTD ...String:
MADPKYADLP GIARNEPDVY ETSDLPEDDQ AEFDAEELTS TSVEHIIVNP NAAYDKFKDK RVGTKGLDFS DRIGKTKRTG YESGEYEML GEGLGVKETP QQKYQRLLHE VQELTTEVEK IKTTVKESAT EEKLTPVLLA KQLAALKQQL VASHLEKLLG P DAAINLTD PDGALAKRLL LQLEATKNSK GGSGGKTTGT PPDSSLVTYE LHSRPEQDKF SQAAKVAELE KRLTELETAV RC DQDAQNP LSAGLQGACL METVELLQAK VSALDLAVLD QVEARLQSVL GKVNEIAKHK ASVEDADTQS KVHQLYETIQ RWS PIASTL PELVQRLVTI KQLHEQAMQF GQLLTHLDTT QQMIANSLKD NTTLLTQVQT TMRENLATVE GNFASIDERM KKLG K

UniProtKB: Dynactin subunit 2

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Macromolecule #10: Dynactin subunit 3

MacromoleculeName: Dynactin subunit 3 / type: protein_or_peptide / ID: 10 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 21.145379 KDa
SequenceString:
MAGLTDLQRL QARVEELERW VYGPGGARGS RKVADGLVKV QVALGNISSK RERVKILYKK IEDLIKYLDP EYIDRIAIPD ASKLQFILA EEQFILSQVA LLEQVNALVP MLDSAHIKAV PEHAARLQRL AQIHIQQQDQ CVEITEESKA LLEEYNKTTM L LSKQFVQW DELLCQLEAA TQVKPAEE

UniProtKB: Dynactin subunit 3

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Macromolecule #11: Dynactin subunit 1

MacromoleculeName: Dynactin subunit 1 / type: protein_or_peptide / ID: 11 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 141.920562 KDa
SequenceString: MAQSKRHVYS RTPSGSRMSA EASARPLRVG SRVEVIGKGH RGTVAYVGAT LFATGKWVGV ILDEAKGKND GTVQGRKYFT CDEGHGIFV RQSQIQVFED GADTTSPETP DSSASKVLKR EGTDTTAKTS KLRGLKPKKA PTARKTTTRR PKPTRPASTG V AGASSSLG ...String:
MAQSKRHVYS RTPSGSRMSA EASARPLRVG SRVEVIGKGH RGTVAYVGAT LFATGKWVGV ILDEAKGKND GTVQGRKYFT CDEGHGIFV RQSQIQVFED GADTTSPETP DSSASKVLKR EGTDTTAKTS KLRGLKPKKA PTARKTTTRR PKPTRPASTG V AGASSSLG PSGSASAGEL SSSEPSTPAQ TPLAAPIIPT PVLTSPGAVP 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 KQAQEKFELS ENCSERP GL RGAAGEQLSF AAGLVYSLSL LQATLHRYEH ALSQCSVDVY KKVGSLYPEM SAHERSLDFL IELLHKDQLD ETVNVEPL T KAIKYYQHLY SIHLAEQPED CTMQLADHIK FTQSALDCMS VEVGRLRAFL QGGQEATDIA LLLRDLETSC SDIRQFCKK IRRRMPGTDA PGIPAALAFG PQVSDTLLDC RKHLTWVVAV LQEVAAAAAQ LIAPLAENEG LLVAALEELA FKASEQIYGT PSSSPYECL RQSCNILIST MNKLATAMQE GEYDAERPPS KPPPVELRAA ALRAEITDAE GLGLKLEDRE TVIKELKKSL K IKGEELSE ANVRLSLLEK KLDSAAKDAD ERIEKVQTRL EETQALLRKK EKEFEETMDA LQADIDQLEA EKAELKQRLN SQ SKRTIEG LRGPPPSGIA TLVSGIAGEE QQRGAIPGQA PGSVPGPGLV KDSPLLLQQI SAMRLHISQL QHENSILKGA QMK ASLASL PPLHVAKLSH EGPGSELPAG ALYRKTSQLL ETLNQLSTHT HVVDITRTSP AAKSPSAQLM EQVAQLKSLS DTVE KLKDE VLKETVSQRP GATVPTDFAT FPSSAFLRAK EEQQDDTVYM GKVTFSCAAG FGQRHRLVLT QEQLHQLHDR LIS

UniProtKB: Dynactin subunit 1

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Macromolecule #12: Dynactin subunit 1, p150-glued

MacromoleculeName: Dynactin subunit 1, p150-glued / type: protein_or_peptide / ID: 12 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 7.08172 KDa
SequenceString: (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) ...String:
(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)

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Macromolecule #13: Dynactin subunit 2, p50 dynamitin

MacromoleculeName: Dynactin subunit 2, p50 dynamitin / type: protein_or_peptide / ID: 13 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 7.42214 KDa
SequenceString: (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) ...String:
(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)

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Macromolecule #14: Dynactin subunit 1

MacromoleculeName: Dynactin subunit 1 / type: protein_or_peptide / ID: 14 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 141.892547 KDa
SequenceString: MAQSKRHVYS RTPSGSRMSA EASARPLRVG SRVEVIGKGH RGTVAYVGAT LFATGKWVGV ILDEAKGKND GTVQGRKYFT CDEGHGIFV RQSQIQVFED GADTTSPETP DSSASKVLKR EGTDTTAKTS KLRGLKPKKA PTARKTTTRR PKPTRPASTG V AGASSSLG ...String:
MAQSKRHVYS RTPSGSRMSA EASARPLRVG SRVEVIGKGH RGTVAYVGAT LFATGKWVGV ILDEAKGKND GTVQGRKYFT CDEGHGIFV RQSQIQVFED GADTTSPETP DSSASKVLKR EGTDTTAKTS KLRGLKPKKA PTARKTTTRR PKPTRPASTG V AGASSSLG PSGSASAGEL SSSEPSTPAQ TPLAAPIIPT PVLTSPGAVP 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 KQAQEKFELS ENCSERP GL RGAAGEQLSF AAGLVYSLSL LQATLHRYEH ALSQCSVDVY KKVGSLYPEM SAHERSLDFL IELLHKDQLD ETVNVEPL T KAIKYYQHLY SIHLAEQPED CTMQLADHIK FTQSALDCMS VEVGRLRAFL QGGQEATDIA LLLRDLETSC SDIRQFCKK IRRRMPGTDA PGIPAALAFG PQVSDTLLDC RKHLTWVVAV LQEVAAAAAQ LIAPLAENEG LLVAALEELA FKASEQIYGT PSSSPYECL RQSCNILIST MNKLATAMQE GEYDAERPPS KPPPVELRAA ALRAEITDAE GLGLKLEDRE TVIKELKKSL K IKGEELSE ANVRLSLLEK KLDSAAKDAD ERIEKVQTRL EETQALLRKK EKEFEETMDA LQADIDQLEA EKAELKQRLN SQ SKRTIEG LRGPPPSGIA TLVSGIAGEE QQRGAIPGQA PGSVPGPGLV KDSPLLLQQI SAMRLHISQL QHENSILKGA QMK ASLASL PPLHVAKLSH EGPGSELPAG ALYRKTSQLL ETLNQLSTHT HVVDITRTSP AAKSPSAQLM EQVAQLKSLS DTVE KLKDE VLKETVSQRP GATVPTDFAT FPSSAFLRAK EEQQDDTVYM GKVTFSCAAG FGQRHRLVLT QEQLHQLHSR LIS

UniProtKB: Dynactin subunit 1

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Macromolecule #15: ADENOSINE-5'-DIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 15 / Number of copies: 8 / 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 #16: PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER

MacromoleculeName: PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / type: ligand / ID: 16 / Number of copies: 1 / Formula: ANP
Molecular weightTheoretical: 506.196 Da
Chemical component information

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

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Macromolecule #17: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 17 / Number of copies: 3 / Formula: ZN
Molecular weightTheoretical: 65.409 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
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 57.7 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.0 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.49 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 45091
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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