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- EMDB-38648: Comamonas testosteroni KF-1 circularly permuted group II intron 2... -
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Open data
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Basic information
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Title | Comamonas testosteroni KF-1 circularly permuted group II intron 2S state | |||||||||
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![]() | CryoEM / Ribozyme / RNA | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.67 Å | |||||||||
![]() | Wang L / Xie JH / Zhang C / Zou J / Huang Z / Shang S / Chen X / Yang Y / Liu J / Dong H ...Wang L / Xie JH / Zhang C / Zou J / Huang Z / Shang S / Chen X / Yang Y / Liu J / Dong H / Huang D / Su Z | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Structural basis of circularly permuted group II intron self-splicing. Authors: Liu Wang / Jiahao Xie / Chong Zhang / Jian Zou / Zirui Huang / Sitong Shang / Xingyu Chen / Yang Yang / Jianquan Liu / Haohao Dong / Dingming Huang / Zhaoming Su / ![]() Abstract: Circularly permuted group II introns (CP introns) consist of rearranged structural domains separated by two tethered exons, generating branched introns and circular exons via back-splicing. ...Circularly permuted group II introns (CP introns) consist of rearranged structural domains separated by two tethered exons, generating branched introns and circular exons via back-splicing. Structural and mechanistic understanding of circular RNA (circRNA) generation by CP introns remains elusive. We resolve cryo-electron microscopy structures of a natural CP intron in different states during back-splicing at a resolution of 2.5-2.9 Å. Domain 6 (D6) undergoes a conformational change of 65° after branching, to facilitate 3'-exon recognition and circularization. Previously unseen tertiary interactions compact the catalytic triad and D6 for splicing without protein, whereas a metal ion, M, is observed to stabilize the 5'-exon during splicing. While these unique features were not observed in canonical group II introns and spliceosomes, they are common in CP introns, as demonstrated by the cryo-EM structure of another CP intron discovered by comparative genomics analysis. Our results elucidate the mechanism of CP intron back-splicing dynamics, with potential applications in circRNA research and therapeutics. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 6.3 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 15.6 KB 15.6 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 10.6 KB | Display | ![]() |
Images | ![]() | 89.9 KB | ||
Filedesc metadata | ![]() | 5.3 KB | ||
Others | ![]() ![]() | 116.1 MB 116.1 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8xtrMC ![]() 8xtpC ![]() 8xtqC ![]() 8xtsC ![]() 9is7C M: atomic model generated by this map C: citing same article ( |
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Links
EMDB pages | ![]() ![]() |
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Map
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.85 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
File | emd_38648_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_38648_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Comamonas testosteroni KF-1 circularly permuted group II intron 2...
Entire | Name: Comamonas testosteroni KF-1 circularly permuted group II intron 2S state |
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Components |
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-Supramolecule #1: Comamonas testosteroni KF-1 circularly permuted group II intron 2...
Supramolecule | Name: Comamonas testosteroni KF-1 circularly permuted group II intron 2S state type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2 |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 251 KDa |
-Macromolecule #1: RNA (219-MER)
Macromolecule | Name: RNA (219-MER) / type: rna / ID: 1 Details: In chain A, resid 140 - resid 210 is missed in our model. Number of copies: 1 |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 70.555961 KDa |
Sequence | String: CCGGGGCGCC ACCCCGGAAG UGAUGCGAGU CGCCAACUCG CAUCACAAGC AAACGCUGUA GCCGCGUGCC UCUAAUAGGG CUGGCGCGG UUGCGAAGGG CGCUGGUGAG UGCAACUCUC ACCUUCGACC CAAUCCAUCU UGCGGCUCAA CCCCGCAAGA U CAUCGCCA ...String: CCGGGGCGCC ACCCCGGAAG UGAUGCGAGU CGCCAACUCG CAUCACAAGC AAACGCUGUA GCCGCGUGCC UCUAAUAGGG CUGGCGCGG UUGCGAAGGG CGCUGGUGAG UGCAACUCUC ACCUUCGACC CAAUCCAUCU UGCGGCUCAA CCCCGCAAGA U CAUCGCCA GACCGCUGGC GGCGUACUGA GUGACAAACG AGGCAAAACC AAAUUGAAGU U GENBANK: GENBANK: CP140157.1 |
-Macromolecule #2: RNA (595-MER)
Macromolecule | Name: RNA (595-MER) / type: rna / ID: 2 / Number of copies: 1 |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 193.64025 KDa |
Sequence | String: GGGCGACCGU GAAACGGCGC UGGGCAGGAA AUGGCCCAGU GACCUGGUCA AUGGUGAAAG UCGGUGAAAG ACCGACCGGU GGGGCGUAU CGAAAGAGCG CAACACCUGC CGCACAGGAU GGCUUCUGAG GUACCGGUGA CGGUACAGAA CGCGGAGGGG A AACCUGGA ...String: GGGCGACCGU GAAACGGCGC UGGGCAGGAA AUGGCCCAGU GACCUGGUCA AUGGUGAAAG UCGGUGAAAG ACCGACCGGU GGGGCGUAU CGAAAGAGCG CAACACCUGC CGCACAGGAU GGCUUCUGAG GUACCGGUGA CGGUACAGAA CGCGGAGGGG A AACCUGGA AGCGAGGGCA CCUCGGGAAA CCGGGGGUCG AUGCAUAGCU CAAACCUGUA ACGGCACCAG UGGAGGGUGC UG UGCGGAG CAACGUGGAG CCACAGGCAU GAAGCCGUGG UUCGUAGUCG AUGAGACAAG CGGUGAGUAA GGGAAGGGCU GCG AACAUC GCCUCCCCGA AAUCCAAGGA AAGCCGAAAG GCUAGCCGCU UUGUUGAGAC AGUGGCGCCA CGUUGCGCAU UAGC CGUGA CCUAAACGGG GAACCUCUUG GCCGUACCGA CUCGGGUGGC ACCGGUCGGG CUCGAUGGCU CAAGAGGGGG AGAUG UGAU GAUUAGGGUU UGACCCGUGA UGCGAUACGA CCGAAGCAUC CGGGGAGCUG UCUGACGAAG AGUCGGCAGC AGUGGG UUU GGCGACCCGC UCCGAAAGUC GCAAGCGUUU GC GENBANK: GENBANK: CP140157.1 |
-Macromolecule #3: POTASSIUM ION
Macromolecule | Name: POTASSIUM ION / type: ligand / ID: 3 / Number of copies: 6 / Formula: K |
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Molecular weight | Theoretical: 39.098 Da |
-Macromolecule #4: MAGNESIUM ION
Macromolecule | Name: MAGNESIUM ION / type: ligand / ID: 4 / Number of copies: 30 / Formula: MG |
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Molecular weight | Theoretical: 24.305 Da |
-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: 7.5 |
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Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
Microscope | TFS KRIOS |
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Image recording | Film or detector model: GATAN K2 QUANTUM (4k x 4k) / Average electron dose: 59.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.5 µm / Nominal defocus min: 0.8 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |