+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-16923 | ||||||||||||||||||||||||
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Title | Human Mitochondrial Lon Y394F Mutant ADP Bound | ||||||||||||||||||||||||
Map data | |||||||||||||||||||||||||
Sample |
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Keywords | Human mitochondrial AAA+ protease / motor protein / HYDROLASE | ||||||||||||||||||||||||
Function / homology | Function and homology information oxidation-dependent protein catabolic process / PH domain binding / endopeptidase La / G-quadruplex DNA binding / response to aluminum ion / mitochondrial DNA metabolic process / mitochondrial genome maintenance / ATP-dependent peptidase activity / protein quality control for misfolded or incompletely synthesized proteins / mitochondrial nucleoid ...oxidation-dependent protein catabolic process / PH domain binding / endopeptidase La / G-quadruplex DNA binding / response to aluminum ion / mitochondrial DNA metabolic process / mitochondrial genome maintenance / ATP-dependent peptidase activity / protein quality control for misfolded or incompletely synthesized proteins / mitochondrial nucleoid / insulin receptor substrate binding / chaperone-mediated protein complex assembly / DNA polymerase binding / regulation of peptidyl-tyrosine phosphorylation / negative regulation of insulin receptor signaling pathway / mitochondrion organization / proteolysis involved in protein catabolic process / response to hormone / ADP binding / protein catabolic process / single-stranded DNA binding / cellular response to oxidative stress / sequence-specific DNA binding / single-stranded RNA binding / response to hypoxia / mitochondrial matrix / serine-type endopeptidase activity / ATP hydrolysis activity / mitochondrion / nucleoplasm / ATP binding / membrane / identical protein binding / cytosol Similarity search - Function | ||||||||||||||||||||||||
Biological species | Homo sapiens (human) | ||||||||||||||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.89 Å | ||||||||||||||||||||||||
Authors | Kereiche S / Bauer JA / Matyas P / Novacek J / Kutejova E | ||||||||||||||||||||||||
Funding support | Slovakia, European Union, Czech Republic, 7 items
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Citation | Journal: To Be Published Title: Phosphorylation of the N-terminal domain of human mitochondrial Lon protease disrupts its functions Authors: Ondrovicova G / Kunova N / Kereiche S / Pinkas M / Krajcovicova V / Bauer JA / Stojkovicova B / Havalova H / Lukacova V / Kohutova L / Martinakova L / Barath P / Novacek J / Kutejova E / Pevala V | ||||||||||||||||||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_16923.map.gz | 140.3 MB | EMDB map data format | |
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Header (meta data) | emd-16923-v30.xml emd-16923.xml | 16 KB 16 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_16923_fsc.xml | 14.6 KB | Display | FSC data file |
Images | emd_16923.png | 144.5 KB | ||
Filedesc metadata | emd-16923.cif.gz | 6.1 KB | ||
Others | emd_16923_half_map_1.map.gz emd_16923_half_map_2.map.gz | 261.9 MB 261.9 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-16923 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-16923 | HTTPS FTP |
-Related structure data
Related structure data | 8okaMC 8om7C M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_16923.map.gz / Format: CCP4 / Size: 282.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.783 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
File | emd_16923_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_16923_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
-Entire : Human mitochondrial Lon protease
Entire | Name: Human mitochondrial Lon protease |
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Components |
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-Supramolecule #1: Human mitochondrial Lon protease
Supramolecule | Name: Human mitochondrial Lon protease / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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Source (natural) | Organism: Homo sapiens (human) / Organelle: mitochondria |
-Macromolecule #1: Lon protease homolog, mitochondrial
Macromolecule | Name: Lon protease homolog, mitochondrial / type: protein_or_peptide / ID: 1 / Number of copies: 6 / Enantiomer: LEVO / EC number: endopeptidase La |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 98.183852 KDa |
Recombinant expression | Organism: Escherichia coli (E. coli) |
Sequence | String: MGHHHHHHDY DIPTTENLYF QGAHMTIPDV FPHLPLIAIT RNPVFPRFIK IIEVKNKKLV ELLRRKVRLA QPYVGVFLKR DDSNESDVV ESLDEIYHTG TFAQIHEMQD LGDKLRMIVM GHRRVHISRQ LEVEPEEPEA ENKHKPRRKS KRGKKEAEDE L SARHPAEL ...String: MGHHHHHHDY DIPTTENLYF QGAHMTIPDV FPHLPLIAIT RNPVFPRFIK IIEVKNKKLV ELLRRKVRLA QPYVGVFLKR DDSNESDVV ESLDEIYHTG TFAQIHEMQD LGDKLRMIVM GHRRVHISRQ LEVEPEEPEA ENKHKPRRKS KRGKKEAEDE L SARHPAEL AMEPTPELPA EVLMVEVENV VHEDFQVTEE VKALTAEIVK TIRDIIALNP LYRESVLQMM QAGQRVVDNP IY LSDMGAA LTGAESHELQ DVLEETNIPK RLYKALSLLK KEFELSKLQQ RLGREVEEKI KQTHRKFLLQ EQLKIIKKEL GLE KDDKDA IEEKFRERLK ELVVPKHVMD VVDEELSKLG LLDNHSSEFN VTRNYLDWLT SIPWGKYSNE NLDLARAQAV LEED HYGME DVKKRILEFI AVSQLRGSTQ GKILCFYGPP GVGKTSIARS IARALNREYF RFSVGGMTDV AEIKGHRRTY VGAMP GKII QCLKKTKTEN PLILIDEVDK IGRGYQGDPS SALLELLDPE QNANFLDHYL DVPVDLSKVL FICTANVTDT IPEPLR DRM EMINVSGYVA QEKLAIAERY LVPQARALCG LDESKAKLSS DVLTLLIKQY CRESGVRNLQ KQVEKVLRKS AYKIVSG EA ESVEVTPENL QDFVGKPVFT VERMYDVTPP GVVMGLAWTA MGGSTLFVET SLRRPQDKDA KGDKDGSLEV TGQLGEVM K ESARIAYTFA RAFLMQHAPA NDYLVTSHIH LHVPEGATPK DGPSAGCTIV TALLSLAMGR PVRQNLAMTG EVSLTGKIL PVGGIKEKTI AAKRAGVTCI VLPAENKKDF YDLAAFITEG LEVHFVEHYR EIFDIAFPDE QAEALAVER UniProtKB: Lon protease homolog, mitochondrial |
-Macromolecule #2: ADENOSINE-5'-DIPHOSPHATE
Macromolecule | Name: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 2 / Number of copies: 6 / Formula: ADP |
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Molecular weight | Theoretical: 427.201 Da |
Chemical component information | ChemComp-ADP: |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TALOS ARCTICA |
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Electron beam | Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 3.0 µm / Nominal defocus min: 2.0 µm |
Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 40.0 e/Å2 |
Experimental equipment | Model: Talos Arctica / Image courtesy: FEI Company |