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Yorodumi- EMDB-65774: Cryo-EM structure of Aspergillus fumigatus ErdS dimer with tRNA(A... -
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Open data
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Basic information
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| Title | Cryo-EM structure of Aspergillus fumigatus ErdS dimer with tRNA(Asp) acceptor stem in an intermediate position toward the ATT active site | |||||||||
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Keywords | tRNA binding / sterol binding / aminoacyltransferase / dimer / RNA BINDING PROTEIN / RNA BINDING PROTEIN-RNA complex | |||||||||
| Function / homology | Function and homology informationaspartate-tRNA ligase / aspartate-tRNA ligase activity / aspartyl-tRNA aminoacylation / aminoacyl-tRNA synthetase multienzyme complex / RNA binding / ATP binding / cytosol Similarity search - Function | |||||||||
| Biological species | ![]() ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.65 Å | |||||||||
Authors | Murayama H / Nishimura M / Kise Y / Itoh Y / Nureki O | |||||||||
| Funding support | Japan, 2 items
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Citation | Journal: To Be PublishedTitle: Structural basis for tRNA-dependent sterol aminoacylation underlying cell membrane integrity Authors: Murayama H / Yakobov N / Mahmoudi N / Sasha L / Zuttion S / Senger B / Huck L / Gamper HB / Ji J / Kleiner RE / Nishimura M / Kise Y / Hou Y-M / Mathieu F / Becker HD / Itoh Y / Fischer F / Nureki O | |||||||||
| History |
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_65774.map.gz | 17.8 MB | EMDB map data format | |
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| Header (meta data) | emd-65774-v30.xml emd-65774.xml | 17.9 KB 17.9 KB | Display Display | EMDB header |
| Images | emd_65774.png | 87.1 KB | ||
| Masks | emd_65774_msk_1.map | 35.3 MB | Mask map | |
| Filedesc metadata | emd-65774.cif.gz | 6.7 KB | ||
| Others | emd_65774_half_map_1.map.gz emd_65774_half_map_2.map.gz | 32.8 MB 32.8 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-65774 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-65774 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9w9gMC ![]() 9w9eC ![]() 9w9fC M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_65774.map.gz / Format: CCP4 / Size: 35.3 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: 1.10667 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Mask #1
| File | emd_65774_msk_1.map | ||||||||||||
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| Density Histograms |
-Half map: #2
| File | emd_65774_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #1
| File | emd_65774_half_map_2.map | ||||||||||||
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| Density Histograms |
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Sample components
-Entire : Cryo-EM structure of Aspergillus fumigatus ErdS dimer with tRNA(A...
| Entire | Name: Cryo-EM structure of Aspergillus fumigatus ErdS dimer with tRNA(Asp) acceptor stem in an intermediate position toward the ATT active site |
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| Components |
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-Supramolecule #1: Cryo-EM structure of Aspergillus fumigatus ErdS dimer with tRNA(A...
| Supramolecule | Name: Cryo-EM structure of Aspergillus fumigatus ErdS dimer with tRNA(Asp) acceptor stem in an intermediate position toward the ATT active site type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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| Source (natural) | Organism: ![]() |
-Macromolecule #1: Aspartate--tRNA ligase, cytoplasmic
| Macromolecule | Name: Aspartate--tRNA ligase, cytoplasmic / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO / EC number: aspartate-tRNA ligase |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 107.780023 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MSIKRALSKI RPKADDDSSK SNLSNGSSPR RSIFSSFLRD RDYVSSSDDG SDDSGSGSLS RNQQKRLARE QRRKQRSRLS EEQQSDDSE RRHKEEIAQA AREETAEMKA RYGELPLLQS TSRPREPRIR LEDISSSSVG QEVFFTARLH IIRRMSARLV F LVFRQRLT ...String: MSIKRALSKI RPKADDDSSK SNLSNGSSPR RSIFSSFLRD RDYVSSSDDG SDDSGSGSLS RNQQKRLARE QRRKQRSRLS EEQQSDDSE RRHKEEIAQA AREETAEMKA RYGELPLLQS TSRPREPRIR LEDISSSSVG QEVFFTARLH IIRRMSARLV F LVFRQRLT TFQGVLHEKP GAKSIAMVQW AEHLRLGSIV RVRGIVQTPQ VPVLGCSIHD VELDVEQIHL VVHREEPVPF SV YEAEIRT AEEDKVEGRR SHLPDRTRLN NRILDLRTPT SQSIFRLQSA LCNIFRSSLD EQGFIEIHTP KLQGSATESG ASV FQVNYF GRDAFLAEAP QLAKQMAIAA DFERVYEIGA VFRAEPAPTA AALTEYTGLD IEMAIEEHYH EMLDVLDAVI KNML KGVYG RYRREIEIVK HQFPSEDVVW LEETPIIRFS DGIKMLNESG WRDEDGNPLP EDDDLHTRDE IRLGELVKEK YGTDY YILD KFPVAARPFF AMPDPEDPRF TNSFDIFIRG QEIVSGGQRI HDPRMLEESM RRSGINPDTM EDYLEGFRWG APPHAG AGV GLERLLMLLL KLGNIRLASL FHRDPKSFPP KPPALLLRHP ESSTIEPPWQ REGRGSLAKD ESELQPLEHL IANYGDA TS TSWGDERFKI WRDMATGAAV SYVPSSNNYA VIPGNPLCDP SQYNRIITQF LQWMRRETKY KPIWLLCSPE VESILGDK L GWRSLSCIAE ERVDPSRNQA ASDGEIARKI RRAENEGIKI VEMKYGEMVP DDVREKIDAR IQDWLANRKG TQVHLSEIH PWRDSEHRWY FYAVDKSGTI CAFVALAMLS PHFGMQVKYS FDFPGSPNGV IEYIVTHAIQ TAARAGTKSL TFGAGATATL TPGHNLHGA KIKMLQHTYE TLAKQFHLVR KSEFRAKLGA HEEPLYIAYP PHGLGSRGIR AVLHFFED UniProtKB: Aspartate--tRNA ligase, cytoplasmic |
-Macromolecule #2: tRNA(Asp)
| Macromolecule | Name: tRNA(Asp) / type: rna / ID: 2 / Number of copies: 1 |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 24.070229 KDa |
| Sequence | String: UCCUCGAUGG UCUAACGGUC AUGAUUUCCG CUUGUCACGC GGGAGACCAG GGUUCGACUC CCUGUCGGGG AGCCA |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 8 |
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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: 51.0 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: 1.6 µm / Nominal defocus min: 0.8 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi



Keywords
Authors
Japan, 2 items
Citation





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Processing
FIELD EMISSION GUN
