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Open data
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Basic information
Entry | ![]() | ||||||||||||||||||||||||||||||
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Title | CryoEM structure of apo M. tuberculosis ClpP1P2 | ||||||||||||||||||||||||||||||
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![]() | Mycobacterium tuberculosis / caseinolytic protease system / holoenzymes / antibiotics / Bortezomib / HYDROLASE | ||||||||||||||||||||||||||||||
Function / homology | ![]() endopeptidase Clp / endopeptidase Clp complex / ATP-dependent peptidase activity / protein quality control for misfolded or incompletely synthesized proteins / peptidoglycan-based cell wall / ATPase binding / serine-type endopeptidase activity / plasma membrane / cytosol Similarity search - Function | ||||||||||||||||||||||||||||||
Biological species | ![]() ![]() ![]() | ||||||||||||||||||||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.69 Å | ||||||||||||||||||||||||||||||
![]() | Zhou B / Gao Y / Zhao H / Chen X / He J / Zhang T / Xiong X | ||||||||||||||||||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Activation mechanism of caseinolytic chaperone-protease system in Mycobacterium tuberculosis by the anti-cancer drug bortezomib Authors: Zhou B / Gao Y / Zhao H / Chen X / He J / Zhang T / Xiong X | ||||||||||||||||||||||||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 59.8 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 16.1 KB 16.1 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 11.7 KB | Display | ![]() |
Images | ![]() | 35 KB | ||
Masks | ![]() | 64 MB | ![]() | |
Filedesc metadata | ![]() | 5.6 KB | ||
Others | ![]() ![]() | 59.5 MB 59.5 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8yd4MC ![]() 8ycxC ![]() 8yd0C ![]() 8yd1C ![]() 8yd2C ![]() 9jvpC ![]() 9jvzC M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Map
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.88 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
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Density Histograms |
-Half map: #2
File | emd_39164_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_39164_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Mycobacterium tuberculosis caseinolytic protease P1P2
Entire | Name: Mycobacterium tuberculosis caseinolytic protease P1P2 |
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Components |
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-Supramolecule #1: Mycobacterium tuberculosis caseinolytic protease P1P2
Supramolecule | Name: Mycobacterium tuberculosis caseinolytic protease P1P2 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() ![]() |
-Macromolecule #1: ATP-dependent Clp protease proteolytic subunit 1
Macromolecule | Name: ATP-dependent Clp protease proteolytic subunit 1 / type: protein_or_peptide / ID: 1 / Number of copies: 7 / Enantiomer: LEVO / EC number: endopeptidase Clp |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 21.727664 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MSQVTDMRSN SQGLSLTDSV YERLLSERII FLGSEVNDEI ANRLCAQILL LAAEDASKDI SLYINSPGGS ISAGMAIYDT MVLAPCDIA TYAMGMAASM GEFLLAAGTK GKRYALPHAR ILMHQPLGGV TGSAADIAIQ AEQFAVIKKE MFRLNAEFTG Q PIERIEAD ...String: MSQVTDMRSN SQGLSLTDSV YERLLSERII FLGSEVNDEI ANRLCAQILL LAAEDASKDI SLYINSPGGS ISAGMAIYDT MVLAPCDIA TYAMGMAASM GEFLLAAGTK GKRYALPHAR ILMHQPLGGV TGSAADIAIQ AEQFAVIKKE MFRLNAEFTG Q PIERIEAD SDRDRWFTAA EALEYGFVDH IITRAHVNGE AQ UniProtKB: ATP-dependent Clp protease proteolytic subunit 1 |
-Macromolecule #2: ATP-dependent Clp protease proteolytic subunit 2
Macromolecule | Name: ATP-dependent Clp protease proteolytic subunit 2 / type: protein_or_peptide / ID: 2 / Number of copies: 7 / Enantiomer: LEVO / EC number: endopeptidase Clp |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 23.562754 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MNSQNSQIQP QARYILPSFI EHSSFGVKES NPYNKLFEER IIFLGVQVDD ASANDIMAQL LVLESLDPDR DITMYINSPG GGFTSLMAI YDTMQYVRAD IQTVCLGQAA SAAAVLLAAG TPGKRMALPN ARVLIHQPSL SGVIQGQFSD LEIQAAEIER M RTLMETTL ...String: MNSQNSQIQP QARYILPSFI EHSSFGVKES NPYNKLFEER IIFLGVQVDD ASANDIMAQL LVLESLDPDR DITMYINSPG GGFTSLMAI YDTMQYVRAD IQTVCLGQAA SAAAVLLAAG TPGKRMALPN ARVLIHQPSL SGVIQGQFSD LEIQAAEIER M RTLMETTL ARHTGKDAGV IRKDTDRDKI LTAEEAKDYG IIDTVLEYRK LSAQTA UniProtKB: ATP-dependent Clp protease proteolytic subunit 2 |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.5 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TALOS ARCTICA |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 60.0 e/Å2 |
Electron beam | Acceleration voltage: 200 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 0.8 µm |
Experimental equipment | ![]() Model: Talos Arctica / Image courtesy: FEI Company |