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Open data
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Basic information
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Title | Structure of the S.aureus MecA protein, in complex with ClpC | |||||||||
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![]() | proteolysis / AAA+ adaptor protein / S.aureus / CHAPERONE | |||||||||
Function / homology | ![]() peptidase activity / cellular response to heat / protein-macromolecule adaptor activity / ATP hydrolysis activity / proteolysis / ATP binding / cytoplasm Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.5 Å | |||||||||
![]() | Carroni M / Azinas S | |||||||||
Funding support | ![]()
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![]() | ![]() Title: ClpC and ClpP act as reciprocal allosteric activators to form a highly efficient AAA+ protease Authors: Azinas S / Wallden K / Katikaridis P / Schahl A / Mogk A / Carroni M | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 89.8 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 21.9 KB 21.9 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 13.9 KB | Display | ![]() |
Images | ![]() | 24.8 KB | ||
Masks | ![]() | 107.2 MB | ![]() | |
Filedesc metadata | ![]() | 6.5 KB | ||
Others | ![]() ![]() ![]() ![]() | 53.7 MB 50.6 MB 99.2 MB 99.2 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 951.7 KB | Display | ![]() |
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Full document | ![]() | 951.2 KB | Display | |
Data in XML | ![]() | 18.3 KB | Display | |
Data in CIF | ![]() | 24.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9goqMC ![]() 9gi1C 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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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.059 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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-Additional map: #2
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-Additional map: #1
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Density Histograms |
-Half map: #2
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Density Histograms |
-Half map: #1
File | emd_51498_half_map_2.map | ||||||||||||
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Density Histograms |
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Sample components
-Entire : N-terminal part of the complex between the AAA+ unfoldase ClpC an...
Entire | Name: N-terminal part of the complex between the AAA+ unfoldase ClpC and the adaptor protein MecA from S.aureus. |
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Components |
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-Supramolecule #1: N-terminal part of the complex between the AAA+ unfoldase ClpC an...
Supramolecule | Name: N-terminal part of the complex between the AAA+ unfoldase ClpC and the adaptor protein MecA from S.aureus. type: complex / ID: 1 / Parent: 0 / Macromolecule list: all Details: This is referred in the paper as the MecA crown and includes only the N-terminal and coiled-coil part of ClpC. |
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Source (natural) | Organism: ![]() ![]() |
-Macromolecule #1: Adapter protein MecA
Macromolecule | Name: Adapter protein MecA / type: protein_or_peptide / ID: 1 / Number of copies: 6 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 28.35417 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MRIERVDDTT VKLFITYSDI EARGFSREDL WTNRKRGEEF FWSMMDEINE EEDFVVEGPL WIQVHAFEKG VEVTISKSKN EDMMNMSDD DATDQFDEQV QELLAQTLEG EDQLEELFEQ RTKEKEAQGS KRQKSSARKN TRTIIVKFND LEDVINYAYH S NPITTEFE ...String: MRIERVDDTT VKLFITYSDI EARGFSREDL WTNRKRGEEF FWSMMDEINE EEDFVVEGPL WIQVHAFEKG VEVTISKSKN EDMMNMSDD DATDQFDEQV QELLAQTLEG EDQLEELFEQ RTKEKEAQGS KRQKSSARKN TRTIIVKFND LEDVINYAYH S NPITTEFE DLLYMVDGTY YYAVYFDSHV DQEVINDSYS QLLEFAYPTD RTEVYLNDYA KIIMSHNVTA QVRRYFPETT E UniProtKB: Adapter protein MecA |
-Macromolecule #2: ATP-dependent Clp protease ATP-binding subunit ClpC
Macromolecule | Name: ATP-dependent Clp protease ATP-binding subunit ClpC / type: protein_or_peptide / ID: 2 / Number of copies: 12 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 91.170352 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MLFGRLTERA QRVLAHAQEE AIRLNHSNIG TEHLLLGLMK EPEGIAAKVL ESFNITEDKV IEEVEKLIGH GQDHVGTLHY TPRAKKVIE LSMDEARKLH HNFVGTEHIL LGLIRENEGV AARVFANLDL NITKARAQVV KALGNPEMSN KNAQASKSNN T PTLDSLAR ...String: MLFGRLTERA QRVLAHAQEE AIRLNHSNIG TEHLLLGLMK EPEGIAAKVL ESFNITEDKV IEEVEKLIGH GQDHVGTLHY TPRAKKVIE LSMDEARKLH HNFVGTEHIL LGLIRENEGV AARVFANLDL NITKARAQVV KALGNPEMSN KNAQASKSNN T PTLDSLAR DLTVIAKDGT LDPVIGRDKE ITRVIEVLSR RTKNNPVLIG EPGVGKTAIA EGLAQAIVNN EVPETLKDKR VM SLDMGTV VAGTKYRGEF EERLKKVMEE IQQAGNVILF IDELHTLVGA GGAEGAIDAS NILKPALARG ELQCIGATTL DEY RKNIEK DAALERRFQP VQVDEPSVVD TVAILKGLRD RYEAHHRINI SDEAIEAAVK LSNRYVSDRF LPDKAIDLID EASS KVRLK SHTTPNNLKE IEQEIEKVKN EKDAAVHAQE FENAANLRDK QTKLEKQYEE AKNEWKNAQN GMSTSLSEED IAEVI AGWT GIPLTKINET ESEKLLSLED TLHERVIGQK DAVNSISKAV RRARAGLKDP KRPIGSFIFL GPTGVGKTEL ARALAE SMF GDDDAMIRVD MSEFMEKHAV SRLVGAPPGY VGHDDGGQLT EKVRRKPYSV ILFDEIEKAH PDVFNILLQV LDDGHLT DT KGRTVDFRNT IIIMTSNVGA QELQDQRFAG FGGSSDGQDY ETIRKTMLKE LKNSFRPEFL NRVDDIIVFH KLTKEELK E IVTMMVNKLT NRLSEQNINI IVTDKAKDKI AEEGYDPEYG ARPLIRAIQK TIEDNLSELI LDGNQIEGKK VTVDHDGKE FKYDIAEQTS ETKTPSQA UniProtKB: ATP-dependent Clp protease ATP-binding subunit ClpC |
-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: 7.4 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | TFS KRIOS |
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Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 40.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 24.0 µm / Nominal defocus min: 0.6 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |