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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 / protein localization to centrosome / positive regulation of norepinephrine uptake / dynein complex / sperm head-tail coupling apparatus / cellular response to cytochalasin B / Formation of the embryonic stem cell BAF (esBAF) complex ...retrograde axonal transport of mitochondrion / dynactin complex / F-actin capping protein complex / WASH complex / protein localization to centrosome / positive regulation of norepinephrine uptake / dynein complex / sperm head-tail coupling apparatus / cellular response to cytochalasin B / Formation of the embryonic stem cell BAF (esBAF) complex / regulation of transepithelial transport / cell junction assembly / Formation of the canonical BAF (cBAF) complex / morphogenesis of a polarized epithelium / Formation of annular gap junctions / Formation of the dystrophin-glycoprotein complex (DGC) / Formation of the polybromo-BAF (pBAF) complex / structural constituent of postsynaptic actin cytoskeleton / Gap junction degradation / GBP-mediated host defense / Formation of neuronal progenitor and neuronal BAF (npBAF and nBAF) / protein localization to adherens junction / barbed-end actin filament capping / Formation of the non-canonical BAF (ncBAF) complex / Cell-extracellular matrix interactions / regulation of G0 to G1 transition / dense body / Tat protein binding / Folding of actin by CCT/TriC / RHOD GTPase cycle / Regulation of CDH1 Function / postsynaptic actin cytoskeleton / apical protein localization / Adherens junctions interactions / Prefoldin mediated transfer of substrate to CCT/TriC / microtubule nucleation / RHOF GTPase cycle / adherens junction assembly / regulation of double-strand break repair / COPI-independent Golgi-to-ER retrograde traffic / Sensory processing of sound by outer hair cells of the cochlea / microtubule associated complex / cytoplasmic dynein complex / tight junction / positive regulation of T cell differentiation / regulation of mitotic metaphase/anaphase transition / Sensory processing of sound by inner hair cells of the cochlea / maintenance of blood-brain barrier / Interaction between L1 and Ankyrins / apical junction complex / spectrin binding / regulation of nucleotide-excision repair / positive regulation of stem cell population maintenance / NuA4 histone acetyltransferase complex / regulation of norepinephrine uptake / transporter regulator activity / Recycling pathway of L1 / positive regulation of double-strand break repair / cortical cytoskeleton / Regulation of MITF-M-dependent genes involved in pigmentation / establishment or maintenance of cell polarity / negative regulation of cell differentiation / nitric-oxide synthase binding / dynein complex binding / brush border / Advanced glycosylation endproduct receptor signaling / EPH-ephrin mediated repulsion of cells / mitotic metaphase chromosome alignment / RHO GTPases Activate WASPs and WAVEs / regulation of synaptic vesicle endocytosis / positive regulation of myoblast differentiation / kinesin binding / regulation of protein localization to plasma membrane / RHO GTPases activate IQGAPs / vesicle-mediated transport / COPI-mediated anterograde transport / positive regulation of double-strand break repair via homologous recombination / regulation of G1/S transition of mitotic cell cycle / axonogenesis / cytoskeleton organization / stress fiber / axon cytoplasm / EPHB-mediated forward signaling / 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 / Recruitment of NuMA to mitotic centrosomes / Anchoring of the basal body to the plasma membrane / substantia nigra development / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation / AURKA Activation by TPX2 / cell motility / calyx of Held / nitric-oxide synthase regulator activity / hippocampal mossy fiber to CA3 synapse / mitotic spindle organization / FCGR3A-mediated phagocytosis / sarcomere 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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| 1 |
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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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