+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-35574 | |||||||||
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Title | Filament interface structure of GAC with phosphate | |||||||||
Map data | ||||||||||
Sample |
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Keywords | Glutaminase / phosphate / filament / PROTEIN FIBRIL / HYDROLASE | |||||||||
Function / homology | Function and homology information glutamine catabolic process / regulation of respiratory gaseous exchange by nervous system process / glutamate biosynthetic process / Glutamate and glutamine metabolism / intracellular glutamate homeostasis / Glutamate Neurotransmitter Release Cycle / glutaminase / glutaminase activity / suckling behavior / TP53 Regulates Metabolic Genes ...glutamine catabolic process / regulation of respiratory gaseous exchange by nervous system process / glutamate biosynthetic process / Glutamate and glutamine metabolism / intracellular glutamate homeostasis / Glutamate Neurotransmitter Release Cycle / glutaminase / glutaminase activity / suckling behavior / TP53 Regulates Metabolic Genes / chemical synaptic transmission / protein homotetramerization / mitochondrial matrix / synapse / mitochondrion / cytosol Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.9 Å | |||||||||
Authors | Guo CJ / Liu JL | |||||||||
Funding support | China, 1 items
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Citation | Journal: Cell Res / Year: 2024 Title: Structural basis for activation and filamentation of glutaminase. Authors: Chen-Jun Guo / Zi-Xuan Wang / Ji-Long Liu / | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_35574.map.gz | 5.5 MB | EMDB map data format | |
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Header (meta data) | emd-35574-v30.xml emd-35574.xml | 13.5 KB 13.5 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_35574_fsc.xml | 7.1 KB | Display | FSC data file |
Images | emd_35574.png | 45.1 KB | ||
Masks | emd_35574_msk_1.map | 30.5 MB | Mask map | |
Filedesc metadata | emd-35574.cif.gz | 5.4 KB | ||
Others | emd_35574_half_map_1.map.gz emd_35574_half_map_2.map.gz | 7.4 MB 7.4 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-35574 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-35574 | HTTPS FTP |
-Validation report
Summary document | emd_35574_validation.pdf.gz | 717 KB | Display | EMDB validaton report |
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Full document | emd_35574_full_validation.pdf.gz | 716.5 KB | Display | |
Data in XML | emd_35574_validation.xml.gz | 11.9 KB | Display | |
Data in CIF | emd_35574_validation.cif.gz | 16.2 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-35574 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-35574 | HTTPS FTP |
-Related structure data
Related structure data | 8imbMC 8imaC 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_35574.map.gz / Format: CCP4 / Size: 5.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Projections & slices | Image control
Images are generated by Spider. generated in cubic-lattice coordinate | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.06 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
File | emd_35574_msk_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_35574_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_35574_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
-Entire : GAC filament with phosphate
Entire | Name: GAC filament with phosphate |
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Components |
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-Supramolecule #1: GAC filament with phosphate
Supramolecule | Name: GAC filament with phosphate / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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Source (natural) | Organism: Homo sapiens (human) |
-Macromolecule #1: Glutaminase kidney isoform, mitochondrial
Macromolecule | Name: Glutaminase kidney isoform, mitochondrial / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO / EC number: glutaminase |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 53.083738 KDa |
Recombinant expression | Organism: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria) |
Sequence | String: LVASGENKIK QGLLPSLEDL LFYTIAEGQE KIPVHKFITA LKSTGLRTSD PRLKECMDML RLTLQTTSDG VMLDKDLFKK CVQSNIVLL TQAFRRKFVI PDFMSFTSHI DELYESAKKQ SGGKVADYIP QLAKFSPDLW GVSVCTVDGQ RHSTGDTKVP F CLQSCVKP ...String: LVASGENKIK QGLLPSLEDL LFYTIAEGQE KIPVHKFITA LKSTGLRTSD PRLKECMDML RLTLQTTSDG VMLDKDLFKK CVQSNIVLL TQAFRRKFVI PDFMSFTSHI DELYESAKKQ SGGKVADYIP QLAKFSPDLW GVSVCTVDGQ RHSTGDTKVP F CLQSCVKP LKYAIAVNDL GTEYVHRYVG KEPSGLRFNK LFLNEDDKPH NPMVNAGAIV VTSLIKQGVN NAEKFDYVMQ FL NKMAGNE YVGFSNATFQ SERESGDRNF AIGYYLKEKK CFPEGTDMVG ILDFYFQLCS IEVTCESASV MAATLANGGF CPI TGERVL SPEAVRNTLS LMHSCGMYDF SGQFAFHVGL PAKSGVAGGI LLVVPNVMGM MCWSPPLDKM GNSVKGIHFC HDLV SLCNF HNYDNLRHFA KKLDPRREGG DQRHSFGPLD YESLQQELAL KETVWKKVSP ESNEDISTTV VYRMESLGEK S UniProtKB: Glutaminase kidney isoform, mitochondrial |
-Macromolecule #2: PHOSPHATE ION
Macromolecule | Name: PHOSPHATE ION / type: ligand / ID: 2 / Number of copies: 4 / Formula: PO4 |
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Molecular weight | Theoretical: 94.971 Da |
Chemical component information | ChemComp-PO4: |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | filament |
-Sample preparation
Buffer | pH: 8.5 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.8 µm / Nominal defocus min: 1.2 µm |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |