+Open data
-Basic information
Entry | Database: SASBDB / ID: SASDCR7 |
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Sample | TET12(1.10)SN-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 #1576 | 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)SN-c6 / Specimen concentration: 0.90-3.60 |
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Buffer | Name: 20 mM Tris 150 mM NaCl 10% glycerol / pH: 7.5 |
Entity #802 | Type: protein / Description: TET12(1.10)SN-c6 / Formula weight: 54.345 / Num. of mol.: 1 / Source: synthetic construct Sequence: MLEEELKQLE EELQAIEEQL AQLQWKAQAR KEKLAQLKEK LGKGDGSPED EIQQLEEEIS QLEQKNSELK EKNQELKYGK GDGDIEQELE RAKESIRRLE QEVNQERSRM QYLQTLLEKG KGDGQLEDKV EELLSKNYHL ENEVERLKKL VGGKGDGLEE ELKQLEEELQ ...Sequence: MLEEELKQLE EELQAIEEQL AQLQWKAQAR KEKLAQLKEK LGKGDGSPED EIQQLEEEIS QLEQKNSELK EKNQELKYGK GDGDIEQELE RAKESIRRLE QEVNQERSRM QYLQTLLEKG KGDGQLEDKV EELLSKNYHL ENEVERLKKL VGGKGDGLEE ELKQLEEELQ AIEEQLAQLQ WKAQARKEKL AQLKEKLGKG DGSPEDEIQQ LEEKNSQLKQ EISQLEEKNQ ELKYGDGKGQ LEDKVEELLS KNYHLENEVE RLKKLVGGDG KGSPEDKISQ LKEKIQQLKQ ENQQLEEENS QLEYGDGKGS PEDENSQLEE KISQLKQKNS ELKEEIQQLE YGDGKGSPED KISELKEENQ QLEQKIQQLK EENSQLEYGK GDGDIEQELE RAKESIRRLE QEVNQERSRM QYLQTLLEKG KGDGSPEDKN SELKEEIQQL EEENQQLEEK ISELKYLEHH HHHHHH |
-Experimental information
Beam | Instrument name: PETRA III P12 / City: Hamburg / 国: Germany / Shape: Point / Type of source: X-ray synchrotron / Wavelength: 0.124 Å / Dist. spec. to detc.: 2 mm | ||||||||||||||||||||||||||||||||||||||||||
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Detector | Name: Pilatus 1M-W / Pixsize x: 0.172 mm | ||||||||||||||||||||||||||||||||||||||||||
Scan | Title: TET12(1.10)SN-c6 / Measurement date: Jun 10, 2016 / Storage temperature: 10 °C / Cell temperature: 20 °C / Exposure time: 0.045 sec. / Number of frames: 20 / Unit: 1/nm /
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Distance distribution function P(R) | Sofotware P(R): GNOM 5.0 / Number of points: 356 /
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Result | Type of curve: single_conc
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