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- EMDB-28800: Structure of an 18mer DegP cage bound to the client protein hTRF1 -
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Open data
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Basic information
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Title | Structure of an 18mer DegP cage bound to the client protein hTRF1 | |||||||||
![]() | Low-resolution cryo-EM map of an 18mer DegP cage bound to the client protein hTRF1. | |||||||||
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Function / homology | ![]() positive regulation of shelterin complex assembly / negative regulation of establishment of protein localization to telomere / negative regulation of establishment of RNA localization to telomere / negative regulation of establishment of protein-containing complex localization to telomere / negative regulation of telomere maintenance via semi-conservative replication / negative regulation of exonuclease activity / negative regulation of telomeric D-loop disassembly / meiotic telomere clustering / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() ![]() ![]() | |||||||||
Method | ![]() ![]() | |||||||||
![]() | Harkness RW / Ripstein ZA / Di Trani JM / Kay LE | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Flexible Client-Dependent Cages in the Assembly Landscape of the Periplasmic Protease-Chaperone DegP. Authors: Robert W Harkness / Zev A Ripstein / Justin M Di Trani / Lewis E Kay / ![]() Abstract: The periplasmic protein DegP, which is implicated in virulence factor transport leading to pathogenicity, is a bi-functional protease and chaperone that helps to maintain protein homeostasis in Gram- ...The periplasmic protein DegP, which is implicated in virulence factor transport leading to pathogenicity, is a bi-functional protease and chaperone that helps to maintain protein homeostasis in Gram-negative bacteria and is essential to bacterial survival under stress conditions. To perform these functions, DegP captures clients inside cage-like structures, which we have recently shown to form through the reorganization of high-order preformed apo oligomers, consisting of trimeric building blocks, that are structurally distinct from client-bound cages. Our previous studies suggested that these apo oligomers may allow DegP to encapsulate clients of various sizes under protein folding stresses by forming ensembles that can include extremely large cage particles, but how this occurs remains an open question. To explore the relation between cage and substrate sizes, we engineered a series of DegP clients of increasing hydrodynamic radii and analyzed their influence on DegP cage formation. We used dynamic light scattering and cryogenic electron microscopy to characterize the hydrodynamic properties and structures of the DegP cages that are adopted in response to each client. We present a series of density maps and structural models that include those for novel particles of approximately 30 and 60 monomers. Key interactions between DegP trimers and the bound clients that stabilize the cage assemblies and prime the clients for catalysis are revealed. We also provide evidence that DegP can form cages which approach subcellular organelles in terms of size. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 14.6 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 16.3 KB 16.3 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 5.5 KB | Display | ![]() |
Images | ![]() | 34.8 KB | ||
Others | ![]() ![]() | 14.5 MB 14.5 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8f1tMC ![]() 8f0aC ![]() 8f0uC ![]() 8f1uC ![]() 8f21C ![]() 8f26C C: citing same article ( M: atomic model generated by this map |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
File | ![]() | ||||||||||||||||||||
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Annotation | Low-resolution cryo-EM map of an 18mer DegP cage bound to the client protein hTRF1. | ||||||||||||||||||||
Voxel size | X=Y=Z: 2.32 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #1
File | emd_28800_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_28800_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Structure of an 18mer DegP cage bound to the client protein hTRF1
Entire | Name: Structure of an 18mer DegP cage bound to the client protein hTRF1 |
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Components |
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-Supramolecule #1: Structure of an 18mer DegP cage bound to the client protein hTRF1
Supramolecule | Name: Structure of an 18mer DegP cage bound to the client protein hTRF1 type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() ![]() ![]() |
-Macromolecule #1: Periplasmic serine endoprotease DegP
Macromolecule | Name: Periplasmic serine endoprotease DegP / type: protein_or_peptide / ID: 1 / Number of copies: 3 / Enantiomer: LEVO / EC number: ![]() |
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Source (natural) | Organism: ![]() ![]() ![]() |
Molecular weight | Theoretical: 36.376176 KDa |
Recombinant expression | Organism: ![]() ![]() ![]() |
Sequence | String: MPSLAPMLEK VMPSVVSINV EGSTTVNTPR MPRNFQQFFG DDSPFCQEGS PFQSSPFCQG GQGGNGGGQQ QKFMALGSGV IIDADKGYV VTNNHVVDNA TVIKVQLSDG RKFDAKMVGK DPRSDIALIQ IQNPKNLTAI KMADSDALRV GDYTVAIGNP F GLGETVTS ...String: MPSLAPMLEK VMPSVVSINV EGSTTVNTPR MPRNFQQFFG DDSPFCQEGS PFQSSPFCQG GQGGNGGGQQ QKFMALGSGV IIDADKGYV VTNNHVVDNA TVIKVQLSDG RKFDAKMVGK DPRSDIALIQ IQNPKNLTAI KMADSDALRV GDYTVAIGNP F GLGETVTS GIVSALGRSG LNAENYENFI QTDAAINRGN AGGALVNLNG ELIGINTAIL APDGGNIGIG FAIPSNMVKN LT SQMVEYG QVKRGELGIM GTELNSELAK AMKVDAQRGA FVSQVLPNSS AAKAGIKAGD VITSLNGKPI SSFAALRAQV GTM PVGSKL TLGLLRDGKQ VNVNLELQQS SQ |
-Macromolecule #2: Periplasmic serine endoprotease DegP
Macromolecule | Name: Periplasmic serine endoprotease DegP / type: protein_or_peptide / ID: 2 / Number of copies: 3 / Enantiomer: LEVO / EC number: ![]() |
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Source (natural) | Organism: ![]() ![]() ![]() |
Molecular weight | Theoretical: 7.970229 KDa |
Recombinant expression | Organism: ![]() ![]() ![]() |
Sequence | String: AEMSNKGKDQ GVVVNNVKTG TPAAQIGLKK GDVIIGANQQ AVKNIAELRK VLDSKPSVLA LNIQRGDSTI YLLMQ |
-Macromolecule #3: Telomeric repeat-binding factor 1
Macromolecule | Name: Telomeric repeat-binding factor 1 / type: protein_or_peptide / ID: 3 / Number of copies: 3 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 3.417168 KDa |
Recombinant expression | Organism: ![]() ![]() ![]() |
Sequence | String: SKILLHYKFN NRTSVMLKDR WRTMKKL |
-Experimental details
-Structure determination
Method | ![]() |
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Aggregation state | particle |
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Sample preparation
Buffer | pH: 7 |
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Vitrification | Cryogen name: ETHANE-PROPANE |
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Electron microscopy
Microscope | FEI TECNAI F20 |
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Electron beam | Acceleration voltage: 200 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD![]() |
Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 35.0 e/Å2 |
Experimental equipment | ![]() Model: Tecnai F20 / Image courtesy: FEI Company |