+Open data
-Basic information
Entry | Database: SASBDB / ID: SASDCY7 |
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Sample | TET12(1.10)S-c6
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Biological species | synthetic construct (others) |
Citation | Journal: Nat Biotechnol / Year: 2017 Title: Design of coiled-coil protein-origami cages that self-assemble in vitro and in vivo. Authors: Ajasja Ljubetič / Fabio Lapenta / Helena Gradišar / Igor Drobnak / Jana Aupič / Žiga Strmšek / Duško Lainšček / Iva Hafner-Bratkovič / Andreja Majerle / Nuša Krivec / Mojca ...Authors: Ajasja Ljubetič / Fabio Lapenta / Helena Gradišar / Igor Drobnak / Jana Aupič / Žiga Strmšek / Duško Lainšček / Iva Hafner-Bratkovič / Andreja Majerle / Nuša Krivec / Mojca Benčina / Tomaž Pisanski / Tanja Ćirković Veličković / Adam Round / José María Carazo / Roberto Melero / Roman Jerala / Abstract: Polypeptides and polynucleotides are natural programmable biopolymers that can self-assemble into complex tertiary structures. We describe a system analogous to designed DNA nanostructures in which ...Polypeptides and polynucleotides are natural programmable biopolymers that can self-assemble into complex tertiary structures. We describe a system analogous to designed DNA nanostructures in which protein coiled-coil (CC) dimers serve as building blocks for modular de novo design of polyhedral protein cages that efficiently self-assemble in vitro and in vivo. We produced and characterized >20 single-chain protein cages in three shapes-tetrahedron, four-sided pyramid, and triangular prism-with the largest containing >700 amino-acid residues and measuring 11 nm in diameter. Their stability and folding kinetics were similar to those of natural proteins. Solution small-angle X-ray scattering (SAXS), electron microscopy (EM), and biophysical analysis confirmed agreement of the expressed structures with the designs. We also demonstrated self-assembly of a tetrahedral structure in bacteria, mammalian cells, and mice without evidence of inflammation. A semi-automated computational design platform and a toolbox of CC building modules are provided to enable the design of protein cages in any polyhedral shape. |
Contact author |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Models
Model #1589 | Type: atomic / Software: (9.16) / Radius of dummy atoms: 1.90 A Search similar-shape structures of this assembly by Omokage search (details) |
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-Sample
Sample | Name: TET12(1.10)S-c6 / Specimen concentration: 2.20-12.90 |
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Buffer | Name: 20 mM Tris 150 mM NaCl 10% glycerol / pH: 7.5 |
Entity #812 | Type: protein / Description: TET12(1.10)S-c6 / Formula weight: 54.546 / Num. of mol.: 1 / Source: synthetic construct Sequence: MELEELEREL QEIEEQLEQL QWKAQERKEK LEQLKEGKGD GSPEDEIQQL EEEISQLEQK NSQLKEKNQQ LKYGGKGDGD IEQELERAKQ SIEELEREVN QERSRMQYLQ TRLSGKGDGR MKQLEDKVEE LERKNYHLEN EVERLKKEVG KGDGELEELE RELQEIEEQL ...Sequence: MELEELEREL QEIEEQLEQL QWKAQERKEK LEQLKEGKGD GSPEDEIQQL EEEISQLEQK NSQLKEKNQQ LKYGGKGDGD IEQELERAKQ SIEELEREVN QERSRMQYLQ TRLSGKGDGR MKQLEDKVEE LERKNYHLEN EVERLKKEVG KGDGELEELE RELQEIEEQL EQLQWKAQER KEKLEQLKEG KGDGSPEDEI QSLEEKNSQL KQEISQLEEK NQQLKYGGDG KGRMKQLEDK VEELERKNYH LENEVERLKK EVGDGKGSPE DKISQLKQKI QQLKQENQQL EEENSQLEYG GDGKGSPEDE NSQLEEKISQ LKQKNSQLKE EIQQLEYGGD GKGSPEDKIS QLKEENQQLE QKIQQLKEEN SQLEYGGKGD GDIEQELERA KQSIEELERE VNQERSRMQY LQTRLSGKGD GSPEDKNSQL KEEIQQLEEE NQQLEEKISQ LKYGLEHHHH HHHH |
-Experimental information
Beam | Instrument name: ESRF BM29 / City: Grenoble / 国: France / Type of source: X-ray synchrotron / Wavelength: 0.1 Å / Dist. spec. to detc.: 2.89 mm | ||||||||||||||||||||||||||||||||||||||||||
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Detector | Name: Pilatus 1M | ||||||||||||||||||||||||||||||||||||||||||
Scan | Title: TET12(1.10)S-c6 / Measurement date: Apr 7, 2016 / Storage temperature: 20 °C / Cell temperature: 20 °C / Exposure time: 2 sec. / Number of frames: 10 / Unit: 1/nm /
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Distance distribution function P(R) | Sofotware P(R): GNOM 5.0 / Number of points: 523 /
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Result | Type of curve: merged
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