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Yorodumi- EMDB-25438: Cryo-EM structure of human NatB in complex with CoA-Alpha-Synuclein -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-25438 | |||||||||
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Title | Cryo-EM structure of human NatB in complex with CoA-Alpha-Synuclein | |||||||||
Map data | ||||||||||
Sample |
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Keywords | NatB / NAA20 / NAA25 / TRANSFERASE / alpha Synuclein | |||||||||
Function / homology | Function and homology information N-terminal peptidyl-glutamine acetylation / N-terminal methionine Nalpha-acetyltransferase NatB / N-terminal peptidyl-aspartic acid acetylation / N-terminal peptidyl-glutamic acid acetylation / NatB complex / N-terminal protein amino acid acetylation / peptide alpha-N-acetyltransferase activity / negative regulation of mitochondrial electron transport, NADH to ubiquinone / neutral lipid metabolic process / regulation of phospholipase activity ...N-terminal peptidyl-glutamine acetylation / N-terminal methionine Nalpha-acetyltransferase NatB / N-terminal peptidyl-aspartic acid acetylation / N-terminal peptidyl-glutamic acid acetylation / NatB complex / N-terminal protein amino acid acetylation / peptide alpha-N-acetyltransferase activity / negative regulation of mitochondrial electron transport, NADH to ubiquinone / neutral lipid metabolic process / regulation of phospholipase activity / negative regulation of monooxygenase activity / regulation of acyl-CoA biosynthetic process / negative regulation of dopamine uptake involved in synaptic transmission / negative regulation of norepinephrine uptake / positive regulation of glutathione peroxidase activity / positive regulation of SNARE complex assembly / positive regulation of hydrogen peroxide catabolic process / supramolecular fiber / negative regulation of transporter activity / negative regulation of chaperone-mediated autophagy / mitochondrial membrane organization / regulation of reactive oxygen species biosynthetic process / positive regulation of protein localization to cell periphery / regulation of synaptic vesicle recycling / negative regulation of platelet-derived growth factor receptor signaling pathway / negative regulation of exocytosis / regulation of glutamate secretion / response to iron(II) ion / regulation of norepinephrine uptake / dopamine biosynthetic process / SNARE complex assembly / positive regulation of neurotransmitter secretion / synaptic vesicle priming / dopamine uptake involved in synaptic transmission / regulation of locomotion / positive regulation of inositol phosphate biosynthetic process / regulation of macrophage activation / mitochondrial ATP synthesis coupled electron transport / negative regulation of microtubule polymerization / synaptic vesicle transport / dynein complex binding / positive regulation of receptor recycling / regulation of dopamine secretion / protein kinase inhibitor activity / negative regulation of thrombin-activated receptor signaling pathway / response to type II interferon / cuprous ion binding / positive regulation of exocytosis / synaptic vesicle exocytosis / positive regulation of endocytosis / cysteine-type endopeptidase inhibitor activity involved in apoptotic process / response to magnesium ion / kinesin binding / regulation of presynapse assembly / alpha-tubulin binding / synaptic vesicle endocytosis / negative regulation of serotonin uptake / localization / phospholipid metabolic process / supramolecular fiber organization / axon terminus / inclusion body / cellular response to copper ion / Hsp70 protein binding / cellular response to epinephrine stimulus / excitatory postsynaptic potential / response to interleukin-1 / adult locomotory behavior / SNARE binding / positive regulation of release of sequestered calcium ion into cytosol / fatty acid metabolic process / long-term synaptic potentiation / regulation of transmembrane transporter activity / ferrous iron binding / protein tetramerization / synapse organization / phosphoprotein binding / regulation of long-term neuronal synaptic plasticity / microglial cell activation / negative regulation of protein kinase activity / phospholipid binding / protein destabilization / PKR-mediated signaling / negative regulation of cysteine-type endopeptidase activity involved in apoptotic process / tau protein binding / positive regulation of protein serine/threonine kinase activity / receptor internalization / synaptic vesicle membrane / positive regulation of inflammatory response / activation of cysteine-type endopeptidase activity involved in apoptotic process / actin cytoskeleton / positive regulation of peptidyl-serine phosphorylation / cellular response to oxidative stress / actin binding / cell cortex / growth cone / histone binding / chemical synaptic transmission / postsynapse / neuron apoptotic process Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.14 Å | |||||||||
Authors | Deng S / Marmorstein R | |||||||||
Funding support | United States, 1 items
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Citation | Journal: Not Published Title: Cryo-EM structure of human NatB in complex with CoA-Alpha-Synuclein Authors: Deng S / Marmorstein R | |||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | EM map: SurfViewMolmilJmol/JSmol |
Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_25438.map.gz | 9.8 MB | EMDB map data format | |
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Header (meta data) | emd-25438-v30.xml emd-25438.xml | 15.4 KB 15.4 KB | Display Display | EMDB header |
Images | emd_25438.png | 168.9 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-25438 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-25438 | HTTPS FTP |
-Related structure data
Related structure data | 7stxMC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_25438.map.gz / Format: CCP4 / Size: 91.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Voxel size | X=Y=Z: 0.83 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Sample components
-Entire : human NatB complex
Entire | Name: human NatB complex |
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Components |
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-Supramolecule #1: human NatB complex
Supramolecule | Name: human NatB complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#3 |
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-Supramolecule #2: N-alpha-acetyltransferase 20, N-alpha-acetyltransferase 25, NatB ...
Supramolecule | Name: N-alpha-acetyltransferase 20, N-alpha-acetyltransferase 25, NatB auxiliary subunit type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1-#2 |
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Source (natural) | Organism: Homo sapiens (human) |
-Supramolecule #3: MDVFM peptide
Supramolecule | Name: MDVFM peptide / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #3 |
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Source (natural) | Organism: Homo sapiens (human) |
-Macromolecule #1: N-alpha-acetyltransferase 20
Macromolecule | Name: N-alpha-acetyltransferase 20 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO EC number: N-terminal methionine Nalpha-acetyltransferase NatB |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 20.390133 KDa |
Recombinant expression | Organism: Spodoptera frugiperda (fall armyworm) |
Sequence | String: MTTLRAFTCD DLFRFNNINL DPLTETYGIP FYLQYLAHWP EYFIVAEAPG GELMGYIMGK AEGSVAREEW HGHVTALSVA PEFRRLGLA AKLMELLEEI SERKGGFFVD LFVRVSNQVA VNMYKQLGYS VYRTVIEYYS ASNGEPDEDA YDMRKALSRD T EKKSIIPL PHPVRPEDIE |
-Macromolecule #2: N-alpha-acetyltransferase 25, NatB auxiliary subunit
Macromolecule | Name: N-alpha-acetyltransferase 25, NatB auxiliary subunit / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 109.64225 KDa |
Recombinant expression | Organism: Spodoptera frugiperda (fall armyworm) |
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)(UNK)(UNK)H CAKVLKAIGL QRTGKQEEA FTLAQEVAAL EPTDDNSLQA ...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)(UNK)(UNK)H CAKVLKAIGL QRTGKQEEA FTLAQEVAAL EPTDDNSLQA LTILYREMHR PELVTKLYEA AVKKVPNSEE YHSHLFMAYA RVGEYKKMQQ AGMALYKIVP KNPYYFWSV MSLIMQSISA QDENLSKTMF LPLAERMVEK MVKEDKIEAE AEVELYYMIL ERLGKYQEAL DVIRGKLGEK L TSEIQSRE NKCMAMYKKL SRWPECNALS RRLLLKNSDD WQFYLTYFDS VFRLIEEAWS PPAEGEHSLE GEVHYSAEKA VK FIEDRIT EESKSSRHLR GPHLAKLELI RRLRSQGCND EYKLGDPEEL MFQYFKKFGD KPCCFTDLKV FVDLLPATQC TKF INQLLG VVPLSTPTED KLALPADIRA LQQHLCVVQL TRLLGLYHTM DKNQKLSVVR ELMLRYQHGL EFGKTCLKTE LQFS DYYCL LAVHALIDVW RETGDETTVW QALTLLEEGL THSPSNAQFK LLLVRIYCML GAFEPVVDLY SSLDAKHIQH DTIGY LLTR YAESLGQYAA ASQSCNFALR FFHSNQKDTS EYIIQAYKYG AFEKIPEFIA FRNRLNNSLH FAQVRTERML LDLLLE ANI STSLAESIKS MNLRPEEDDI PWEDLRDNRD LNVFFSWDPK DRDVSEEHKK LSLEEETLWL RIRSLTLRLI SGLPSLN HP VEPKNSEKTA ENGVSSRIDI LRLLLQQLEA TLETGKRFIE KDIQYPFLGP VPTRMGGFFN SGCSQCQISS FYLVNDIY E LDTSGLEDTM EIQERIENSF KSLLDQLKDV FSKCKGDLLE VKDGNLKTHP TLLENLVFFV ETISVILWVS SYCESVLRP YKLNLQKKKK KKKETSIIMP PVFTSFQDYV TGLQTLISNV VDHIKGLETH LIALKLEELI LEDTSLSPEE RKFSKTVQGK VQSSYLHSL LEMGELLKKR LETTKKLKI |
-Macromolecule #3: Alpha-synuclein
Macromolecule | Name: Alpha-synuclein / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 641.799 Da |
Recombinant expression | Organism: Escherichia coli (E. coli) |
Sequence | String: MDVFM |
-Macromolecule #4: COENZYME A
Macromolecule | Name: COENZYME A / type: ligand / ID: 4 / Number of copies: 1 / Formula: COA |
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Molecular weight | Theoretical: 767.534 Da |
Chemical component information | ChemComp-COA: |
-Macromolecule #5: ACETYL GROUP
Macromolecule | Name: ACETYL GROUP / type: ligand / ID: 5 / Number of copies: 1 / Formula: ACE |
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Molecular weight | Theoretical: 44.053 Da |
Chemical component information | ChemComp-ACE: |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Concentration | 1.0 mg/mL | ||||||||||||
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Buffer | pH: 7 Component:
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Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 289 K / Instrument: FEI VITROBOT MARK II |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy |
Image recording | #0 - Image recording ID: 1 / #0 - Film or detector model: GATAN K3 (6k x 4k) / #0 - Average electron dose: 1.6 e/Å2 / #1 - Image recording ID: 2 / #1 - Film or detector model: GATAN K3 (6k x 4k) / #1 - Average electron dose: 1.3 e/Å2 |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
Startup model | Type of model: NONE |
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Initial angle assignment | Type: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 3.0) |
Final angle assignment | Type: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 3.0) |
Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.14 Å / Resolution method: OTHER / Software - Name: RELION (ver. 3.0) / Details: not sure exactly how many particles were used / Number images used: 726923 |
Image recording ID | 1 |
-Atomic model buiding 1
Refinement | Space: REAL / Protocol: AB INITIO MODEL |
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Output model | PDB-7stx: |