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Yorodumi- PDB-9b85: Cryo-EM structure of human dynactin complex bound to Chlamydia ef... -
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Basic information
| Entry | Database: PDB / ID: 9b85 | ||||||
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| Title | Cryo-EM structure of human dynactin complex bound to Chlamydia effector Dre1 | ||||||
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Keywords | MOTOR PROTEIN / Human dynactin / Chlamydia effector / host-pathogen interaction | ||||||
| Function / homology | Function and homology informationretrograde axonal transport of mitochondrion / dynactin complex / F-actin capping protein complex / WASH complex / positive regulation of norepinephrine uptake / dynein complex / Formation of the embryonic stem cell BAF (esBAF) complex / bBAF complex / cellular response to cytochalasin B / npBAF complex ...retrograde axonal transport of mitochondrion / dynactin complex / F-actin capping protein complex / WASH complex / positive regulation of norepinephrine uptake / dynein complex / Formation of the embryonic stem cell BAF (esBAF) complex / bBAF complex / cellular response to cytochalasin B / npBAF complex / brahma complex / nBAF complex / Formation of the canonical BAF (cBAF) complex / regulation of transepithelial transport / Formation of neuronal progenitor and neuronal BAF (npBAF and nBAF) / Formation of the polybromo-BAF (pBAF) complex / morphogenesis of a polarized epithelium / Formation of annular gap junctions / Formation of the dystrophin-glycoprotein complex (DGC) / structural constituent of postsynaptic actin cytoskeleton / Formation of the non-canonical BAF (ncBAF) complex / cell junction assembly / Gap junction degradation / GBAF complex / Cell-extracellular matrix interactions / regulation of G0 to G1 transition / protein localization to adherens junction / melanosome transport / barbed-end actin filament capping / dense body / Folding of actin by CCT/TriC / Tat protein binding / actin polymerization or depolymerization / coronary vasculature development / postsynaptic actin cytoskeleton / RSC-type complex / RHOD GTPase cycle / Regulation of CDH1 Function / regulation of double-strand break repair / regulation of nucleotide-excision repair / Prefoldin mediated transfer of substrate to CCT/TriC / protein localization to centrosome / regulation of cell morphogenesis / Adherens junctions interactions / RHOF GTPase cycle / adherens junction assembly / apical protein localization / COPI-independent Golgi-to-ER retrograde traffic / Sensory processing of sound by outer hair cells of the cochlea / Interaction between L1 and Ankyrins / microtubule associated complex / regulation of mitotic metaphase/anaphase transition / SWI/SNF complex / cytoplasmic dynein complex / tight junction / lamellipodium assembly / Sensory processing of sound by inner hair cells of the cochlea / ventricular septum development / aorta development / positive regulation of T cell differentiation / mitotic metaphase chromosome alignment / apical junction complex / spectrin binding / positive regulation of double-strand break repair / regulation of norepinephrine uptake / transporter regulator activity / maintenance of blood-brain barrier / positive regulation of stem cell population maintenance / NuA4 histone acetyltransferase complex / establishment or maintenance of cell polarity / Regulation of MITF-M-dependent genes involved in pigmentation / cortical cytoskeleton / Recycling pathway of L1 / dynein complex binding / nitric-oxide synthase binding / regulation of G1/S transition of mitotic cell cycle / Advanced glycosylation endproduct receptor signaling / brush border / sperm head-tail coupling apparatus / EPH-ephrin mediated repulsion of cells / negative regulation of cell differentiation / RHO GTPases Activate WASPs and WAVEs / regulation of synaptic vesicle endocytosis / positive regulation of myoblast differentiation / kinesin binding / RHO GTPases activate IQGAPs / regulation of protein localization to plasma membrane / positive regulation of double-strand break repair via homologous recombination / COPI-mediated anterograde transport / vesicle-mediated transport / stress fiber / EPHB-mediated forward signaling / axon cytoplasm / cytoskeleton organization / Loss of Nlp from mitotic centrosomes / Loss of proteins required for interphase microtubule organization from the centrosome / Recruitment of mitotic centrosome proteins and complexes / MHC class II antigen presentation / axonogenesis / substantia nigra development Similarity search - Function | ||||||
| Biological species | Homo sapiens (human) | ||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.47 Å | ||||||
Authors | Pawar, K.I. / Verba, K.A. | ||||||
| Funding support | 1items
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Citation | Journal: Cell Rep / Year: 2025Title: 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. | ||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 9b85.cif.gz | 1.9 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9b85.ent.gz | 1.5 MB | Display | PDB format |
| PDBx/mmJSON format | 9b85.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/b8/9b85 ftp://data.pdbj.org/pub/pdb/validation_reports/b8/9b85 | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 44333MC ![]() 9b7jC M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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Components
-Protein , 3 types, 10 molecules ABCDEFGIHJ
| #1: Protein | Mass: 42670.688 Da / Num. of mol.: 8 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P61163#2: Protein | | Mass: 41782.660 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P60709#3: Protein | | Mass: 46360.863 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9NZ32 |
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-Dynactin subunit ... , 4 types, 7 molecules KLMPQpq
| #4: Protein | Mass: 52409.016 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9UJW0 |
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| #5: Protein | Mass: 20150.533 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9BTE1 |
| #6: Protein | Mass: 20769.002 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O00399 |
| #9: Protein | Mass: 44285.891 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q13561 |
-F-actin-capping protein subunit ... , 2 types, 2 molecules NO
| #7: Protein | Mass: 32964.727 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P52907 |
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| #8: Protein | Mass: 30669.768 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P47756 |
-Non-polymers , 3 types, 12 molecules 




| #10: Chemical | ChemComp-ADP / #11: Chemical | ChemComp-ANP / | #12: Chemical | |
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-Details
| Has ligand of interest | N |
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| Has protein modification | N |
-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
| Component | Name: Human dynactin complex bound to Chlamydia effector Dre1 Type: COMPLEX / Entity ID: all / Source: NATURAL |
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| Molecular weight | Value: 1.1 MDa / Experimental value: NO |
| Source (natural) | Organism: Homo sapiens (human) |
| Buffer solution | pH: 7.5 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: FEI TITAN KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 1000 nm |
| Image recording | Electron dose: 57.7 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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| 3D reconstruction | Resolution: 3.47 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 50376 / Symmetry type: POINT |
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