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Open data
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Basic information
Entry | Database: PDB / ID: 9d5n | |||||||||||||||||||||
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Title | 48-nm doublet microtubule from Trichomonas vaginalis strain G3 | |||||||||||||||||||||
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![]() | STRUCTURAL PROTEIN / doublet microtubule / tubulin / flagella | |||||||||||||||||||||
Function / homology | ![]() cilium-dependent cell motility / regulation of cilium beat frequency involved in ciliary motility / axonemal microtubule / nucleoside-diphosphate kinase / UTP biosynthetic process / CTP biosynthetic process / motile cilium / nucleoside diphosphate kinase activity / GTP biosynthetic process / positive regulation of cell motility ...cilium-dependent cell motility / regulation of cilium beat frequency involved in ciliary motility / axonemal microtubule / nucleoside-diphosphate kinase / UTP biosynthetic process / CTP biosynthetic process / motile cilium / nucleoside diphosphate kinase activity / GTP biosynthetic process / positive regulation of cell motility / mitotic cytokinesis / axoneme / cilium assembly / alpha-tubulin binding / Hsp70 protein binding / mitotic spindle organization / meiotic cell cycle / Hsp90 protein binding / structural constituent of cytoskeleton / microtubule cytoskeleton organization / mitotic spindle / mitotic cell cycle / microtubule / cytoskeleton / hydrolase activity / calmodulin binding / ciliary basal body / cilium / GTPase activity / GTP binding / ATP binding / nucleus / cytoplasm Similarity search - Function | |||||||||||||||||||||
Biological species | ![]() | |||||||||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.2 Å | |||||||||||||||||||||
![]() | Stevens, A. / Zhou, H.Z. / Kashyap, S. / Crofut, E.J. | |||||||||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Structures of Native Doublet Microtubules from Trichomonas vaginalis Reveal Parasite-Specific Proteins. Authors: Alexander Stevens / Saarang Kashyap / Ethan H Crofut / Shuqi E Wang / Katherine A Muratore / Patricia J Johnson / Z Hong Zhou / ![]() Abstract: Doublet microtubules (DMTs) are flagellar components required for the protist Trichomonas vaginalis (Tv) to swim through the human genitourinary tract to cause trichomoniasis, the most common non- ...Doublet microtubules (DMTs) are flagellar components required for the protist Trichomonas vaginalis (Tv) to swim through the human genitourinary tract to cause trichomoniasis, the most common non-viral sexually transmitted disease. Lack of structures of Tv's DMT (Tv-DMT) has prevented structure-guided drug design to manage Tv infection. Here, we determine the 16 nm, 32 nm, 48 nm and 96 nm-repeat structures of native Tv-DMT at resolution ranging from 3.4 to 4.4 Å by cryogenic electron microscopy (cryoEM) and built an atomic model for the entire Tv-DMT. These structures show that Tv-DMT is composed of 30 different proteins, including the α- and β-tubulin, 19 microtubule inner proteins (MIPs) and 9 microtubule outer proteins. While the A-tubule of Tv-DMT is simplistic compared to DMTs of other organisms, the B-tubule of Tv-DMT features parasite-specific proteins, such as TvFAP40 and TvFAP35. Notably, TvFAP40 and TvFAP35 form filaments near the inner and outer junctions, respectively, and interface with stabilizing MIPs. This atomic model of the Tv-DMT highlights diversity of eukaryotic motility machineries and provides a structural framework to inform rational design of therapeutics against trichomoniasis. | |||||||||||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 30 MB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 46580MC ![]() 45999 ![]() 46000 ![]() 46001 ![]() 46007 ![]() 46008 ![]() 46010 ![]() 46011 ![]() 46012 ![]() 46013 ![]() 46014 ![]() 46015 ![]() 46016 ![]() 46017 ![]() 46018 ![]() 46019 ![]() 46022 ![]() 46025 ![]() 46027 ![]() 46036 C: citing same article ( M: map data used to model this data |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Components
-Protein , 16 types, 425 molecules 0FlFmFnFoFpFqFrFsA0FtFuFvFwFxFyFzGHGUGVGWGXGYGZGaGbGcGdGeGf...
#1: Protein | Mass: 50001.035 Da / Num. of mol.: 191 / Source method: isolated from a natural source / Source: (natural) ![]() #2: Protein | | Mass: 43119.344 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #3: Protein | Mass: 50166.504 Da / Num. of mol.: 188 / Source method: isolated from a natural source / Source: (natural) ![]() #4: Protein | Mass: 35480.570 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #5: Protein | Mass: 46130.445 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #6: Protein | Mass: 43785.008 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #11: Protein | Mass: 54623.988 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #13: Protein | Mass: 28259.299 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #14: Protein | Mass: 32057.600 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #15: Protein | Mass: 107833.578 Da / Num. of mol.: 7 / Source method: isolated from a natural source / Source: (natural) ![]() #17: Protein | Mass: 42253.996 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() #18: Protein | Mass: 28401.012 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #19: Protein | | Mass: 8949.297 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #20: Protein | | Mass: 12391.051 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #21: Protein | Mass: 59697.285 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #22: Protein | Mass: 68197.602 Da / Num. of mol.: 7 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Parkin co-regulated ... , 2 types, 7 molecules HAHBHCHDC2C3Cz
#7: Protein | Mass: 27685.980 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #12: Protein | Mass: 27272.264 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Cilia- and flagella-associated protein ... , 4 types, 19 molecules ICJCKCLMC1CICuCvCwCxCyNCVCXCHCdCeD
#8: Protein | Mass: 55181.746 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #9: Protein | Mass: 22837.334 Da / Num. of mol.: 8 / Source method: isolated from a natural source / Source: (natural) ![]() #10: Protein | Mass: 57844.656 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() #16: Protein | Mass: 65743.289 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Non-polymers , 3 types, 567 molecules 




#23: Chemical | ChemComp-GDP / #24: Chemical | ChemComp-GTP / #25: Chemical | ChemComp-MG / |
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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: doublet microtubule with microtubule inner proteins / Type: COMPLEX / Details: from T. vaginalis / Entity ID: #1, #3 / Source: NATURAL | |||||||||||||||||||||||||
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Molecular weight | Value: 20.1 MDa / Experimental value: NO | |||||||||||||||||||||||||
Source (natural) | Organism: ![]() | |||||||||||||||||||||||||
Buffer solution | pH: 7.4 Details: 150 mM NaCl, 50 mM 325 Tris, 2 mM MgCl2, 1 mM DTT, 5 mM ATP 2 x complete protease inhibitor, pH 7.4 | |||||||||||||||||||||||||
Buffer component |
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Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | |||||||||||||||||||||||||
Specimen support | Grid material: COPPER / Grid mesh size: 200 divisions/in. / Grid type: Quantifoil R2/1 | |||||||||||||||||||||||||
Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE-PROPANE / Humidity: 100 % / Chamber temperature: 281 K |
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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: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 81000 X / Nominal defocus max: 2000 nm / Nominal defocus min: 1200 nm / Calibrated defocus min: 1200 nm / Calibrated defocus max: 2000 nm / Cs: 2.7 mm / Alignment procedure: COMA FREE |
Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
Image recording | Electron dose: 45 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
EM software | Name: PHENIX / Version: 1.21.1_5286 / Category: model refinement |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
Particle selection | Num. of particles selected: 941307 |
Symmetry | Point symmetry: C1 (asymmetric) |
3D reconstruction | Resolution: 4.2 Å / Resolution method: OTHER / Num. of particles: 409692 / Algorithm: FOURIER SPACE / Num. of class averages: 3 / Symmetry type: POINT |
Atomic model building | Protocol: FLEXIBLE FIT / Space: REAL |
Atomic model building | Source name: AlphaFold / Type: in silico model |