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- EMDB-52840: Structure of the Mycobacterium Tuberculosis ClpC1P1P2 complex bou... -
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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | Structure of the Mycobacterium Tuberculosis ClpC1P1P2 complex bound to the activator Bz-Leu-Leu | |||||||||
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![]() | protein quality control / peptide activator / protease / ATPase / CHAPERONE | |||||||||
Function / homology | ![]() endopeptidase Clp / endopeptidase Clp complex / ATP-dependent peptidase activity / protein quality control for misfolded or incompletely synthesized proteins / protein folding chaperone / peptidoglycan-based cell wall / ATPase binding / serine-type endopeptidase activity / protein homodimerization activity / ATP hydrolysis activity ...endopeptidase Clp / endopeptidase Clp complex / ATP-dependent peptidase activity / protein quality control for misfolded or incompletely synthesized proteins / protein folding chaperone / peptidoglycan-based cell wall / ATPase binding / serine-type endopeptidase activity / protein homodimerization activity / ATP hydrolysis activity / ATP binding / plasma membrane / cytosol Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.09 Å | |||||||||
![]() | Weinhaeupl K / Semchonok D / Gragera M / Arranz R / Bueno Carrasco MT / Fraga H | |||||||||
Funding support | 1 items
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![]() | ![]() Title: Structure of the Mycobacterium Tuberculosis ClpC1P1P2 complex bound to the activator Bz-Leu-Leu Authors: Weinhaeupl K / Semchonok DA / Gragera M / Arranz R / Bueno Carrasco MT / Fraga H | |||||||||
History |
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Structure visualization
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Downloads & links
-EMDB archive
Map data | ![]() | 655.5 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 20 KB 20 KB | Display Display | ![]() |
Images | ![]() | 28.5 KB | ||
Filedesc metadata | ![]() | 6.8 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 536.3 KB | Display | ![]() |
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Full document | ![]() | 535.9 KB | Display | |
Data in XML | ![]() | 8.2 KB | Display | |
Data in CIF | ![]() | 9.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9if4MC 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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Related items in Molecule of the Month |
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Map
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Voxel size | X=Y=Z: 0.525 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
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Sample components
-Entire : ClpC1P1P2
Entire | Name: ClpC1P1P2 |
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Components |
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-Supramolecule #1: ClpC1P1P2
Supramolecule | Name: ClpC1P1P2 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#5 |
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Source (natural) | Organism: ![]() ![]() |
-Macromolecule #1: ATP-dependent Clp protease ATP-binding subunit ClpC1
Macromolecule | Name: ATP-dependent Clp protease ATP-binding subunit ClpC1 / type: protein_or_peptide / ID: 1 / Number of copies: 6 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 73.57568 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: SLVLDQFGRN LTAAAMEGKL DPVIGREKEI ERVMQVLSRR TKNNPVLIGE PGVGKTAVVE GLAQAIVHGE VPETLKDKQL YTLDLGSLV AGSRYRGDFE ERLKKVLKEI NTRGDIILFI DELHTLVGAG AAEGAIDAAS ILKPKLARGE LQTIGATTLD E YRKYIEKD ...String: SLVLDQFGRN LTAAAMEGKL DPVIGREKEI ERVMQVLSRR TKNNPVLIGE PGVGKTAVVE GLAQAIVHGE VPETLKDKQL YTLDLGSLV AGSRYRGDFE ERLKKVLKEI NTRGDIILFI DELHTLVGAG AAEGAIDAAS ILKPKLARGE LQTIGATTLD E YRKYIEKD AALERRFQPV QVGEPTVEHT IEILKGLRDR YEAHHRVSIT DAAMVAAATL ADRYINDRFL PDKAIDLIDE AG ARMRIRR MTAPPDLREF DEKIAEARRE KESAIDAQDF EKAASLRDRE KTLVAQRAER EKQWRSGDLD VVAEVDDEQI AEV LGNWTG IPVFKLTEAE TTRLLRMEEE LHKRIIGQED AVKAVSKAIR RTRAGLKDPK RPSGSFIFAG PSGVGKTELS KALA NFLFG DDDALIQIDM GEFHDRFTAS RLFGAPPGYV GYEEGGQLTE KVRRKPFSVV LFDEIEKAHQ EIYNSLLQVL EDGRL TDGQ GRTVDFKNTV LIFTSNLGTS DISKPVGLGF SKGGGENDYE RMKQKVNDEL KKHFRPEFLN RIDDIIVFHQ LTREEI IRM VDLMISRVAG QLKSKDMALV LTDAAKALLA KRGFDPVLGA RPLRRTIQRE IEDQLSEKIL FEEVGPGQVV TVDVDNW DG EGPGEDAVFT FTGTRK UniProtKB: ATP-dependent Clp protease ATP-binding subunit ClpC1 |
-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: 21.914957 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: ILPSFIEHSS FGVKESNPYN KLFEERIIFL GVQVDDASAN DIMAQLLVLE SLDPDRDITM YINSPGGGFT SLMAIYDTMQ YVRADIQTV CLGQAASAAA VLLAAGTPGK RMALPNARVL IHQPSLSGVI QGQFSDLEIQ AAEIERMRTL METTLARHTG K DAGVIRKD ...String: ILPSFIEHSS FGVKESNPYN KLFEERIIFL GVQVDDASAN DIMAQLLVLE SLDPDRDITM YINSPGGGFT SLMAIYDTMQ YVRADIQTV CLGQAASAAA VLLAAGTPGK RMALPNARVL IHQPSLSGVI QGQFSDLEIQ AAEIERMRTL METTLARHTG K DAGVIRKD TDRDKILTAE EAKDYGIIDT VLEYRKLSAQ TA UniProtKB: ATP-dependent Clp protease proteolytic subunit 2 |
-Macromolecule #3: ATP-dependent Clp protease proteolytic subunit 1
Macromolecule | Name: ATP-dependent Clp protease proteolytic subunit 1 / type: protein_or_peptide / ID: 3 / Number of copies: 7 / Enantiomer: LEVO / EC number: endopeptidase Clp |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 19.49627 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: LSLTDSVYER LLSERIIFLG SEVNDEIANR LCAQILLLAA EDASKDISLY INSPGGSISA GMAIYDTMVL APCDIATYAM GMAASMGEF LLAAGTKGKR YALPHARILM HQPLGGVTGS AADIAIQAEQ FAVIKKEMFR LNAEFTGQPI ERIEADSDRD R WFTAAEAL EYGFVDHIIT R UniProtKB: ATP-dependent Clp protease proteolytic subunit 1 |
-Macromolecule #4: activator Bz-Leu-Leu
Macromolecule | Name: activator Bz-Leu-Leu / type: protein_or_peptide / ID: 4 / Number of copies: 7 / Enantiomer: LEVO |
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Source (natural) | Organism: synthetic construct (others) |
Molecular weight | Theoretical: 348.437 Da |
Sequence | String: (S0R)L |
-Macromolecule #5: Unknown peptide
Macromolecule | Name: Unknown peptide / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 2.230741 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) |
-Macromolecule #6: ADENOSINE-5'-DIPHOSPHATE
Macromolecule | Name: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 6 / Number of copies: 4 / Formula: ADP |
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Molecular weight | Theoretical: 427.201 Da |
Chemical component information | ![]() ChemComp-ADP: |
-Macromolecule #7: ADENOSINE-5'-TRIPHOSPHATE
Macromolecule | Name: ADENOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 7 / Number of copies: 8 / Formula: ATP |
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Molecular weight | Theoretical: 507.181 Da |
Chemical component information | ![]() ChemComp-ATP: |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Concentration | 1.5 mg/mL |
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Buffer | pH: 7.4 |
Grid | Model: Quantifoil R1.2/1.3 / Material: COPPER/RHODIUM / Mesh: 300 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 30 sec. |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 95 % / Chamber temperature: 277.15 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
Microscope | FEI TALOS ARCTICA |
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Temperature | Min: 77.0 K / Max: 77.0 K |
Image recording | Film or detector model: TFS FALCON 4i (4k x 4k) / Average electron dose: 46.0 e/Å2 |
Electron beam | Acceleration voltage: 200 kV / Electron source: ![]() |
Electron optics | Illumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.2 µm / Nominal defocus min: 0.8 µm |
Sample stage | Specimen holder model: OTHER / Cooling holder cryogen: NITROGEN |
Experimental equipment | ![]() Model: Talos Arctica / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
Refinement | Space: REAL / Protocol: RIGID BODY FIT |
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Output model | ![]() PDB-9if4: |