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Open data
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Basic information
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Title | Paracandidimonas lactea CP group II intron 2S state | |||||||||||||||
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![]() | CryoEM / Ribozyme / RNA | |||||||||||||||
Biological species | ![]() | |||||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.87 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 | ![]() | 6.4 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 15.8 KB 15.8 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 10.6 KB | Display | ![]() |
Images | ![]() | 87.9 KB | ||
Filedesc metadata | ![]() | 5.3 KB | ||
Others | ![]() ![]() | 116.1 MB 116.1 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9is7MC ![]() 8xtpC ![]() 8xtqC ![]() 8xtrC ![]() 8xtsC 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_60833_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_60833_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Paracandidimonas lactea CP group II intron 2S state
Entire | Name: Paracandidimonas lactea CP group II intron 2S state |
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Components |
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-Supramolecule #1: Paracandidimonas lactea CP group II intron 2S state
Supramolecule | Name: Paracandidimonas lactea CP 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: 227 KDa |
-Macromolecule #1: RNA (153-MER)
Macromolecule | Name: RNA (153-MER) / type: rna / ID: 1 / Details: Residues 111-140 is missed in this model / Number of copies: 1 |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 49.428504 KDa |
Sequence | String: AGCAGGCGCC ACCUGCUGCG GAACCGCUGA AGCCGCGUGC CUCUAACAGG GCUGGCGCGG CUACGAAGGG CGCUGGGGGU GGGAACCAC CUCCUUCGAC CCAAUCCAUG GCCUGCGCCG CAACGUGCAG GCCAGCAGUC UCCACGACAA GGAG |
-Macromolecule #2: RNA (582-MER)
Macromolecule | Name: RNA (582-MER) / type: rna / ID: 2 / Number of copies: 1 |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 189.407531 KDa |
Sequence | String: GGGCGACUAC GAAACGGGCC UGGGUAGGAA AUGACCCAGU GACCCUGACA GUUUGGGAAA GUCGGUGAAA GCCCGACCCU CGGGGCCUA GCGAAAGUGG GCGACGAGUG CAACACCUGG AGGCUGAGGG CGUCAGUGAU GGCGUCAGGC AUGCGGGAGA A AUCUAGGC ...String: GGGCGACUAC GAAACGGGCC UGGGUAGGAA AUGACCCAGU GACCCUGACA GUUUGGGAAA GUCGGUGAAA GCCCGACCCU CGGGGCCUA GCGAAAGUGG GCGACGAGUG CAACACCUGG AGGCUGAGGG CGUCAGUGAU GGCGUCAGGC AUGCGGGAGA A AUCUAGGC AUGCUGGCAC CUAUCGAAAG AUGGGGCCGC UGGAUAGCUC AAUCAGGUAA AGGCACCGUU CAGGUGCUGU GU UGAGGCA UAGGAAGGCA GGGCCGCAGU CGCGGUAAGC AAGCAGCGUU GAAGCGCAUC GGCAGUACCG CAUCCGUUAU GGA ACCUUG GGAGCGAGAA ACCCUGGAAA CGGGGGUAGG GUCAGAGACC UAGAUAAAUC CGAUGUGGCC GAGCUGGCUG UCGU UCGAU GCCGUAGUAC UGACUGUCUA AGUAGGGAAG GUCUCGGCAG AUCGUGGGGG UGGCACCCUG CGAAAUUAUC UGCCA AGAC UGGGAGAUGG CUUGAGUAGU GCCGCCGCGC GAGCGGUGGG CAGACCAUGG GGGCAGACUU GCUGGAUGUU CCUAUC GGC GAAAGAGCCA AGCGGUAAC |
-Macromolecule #3: MAGNESIUM ION
Macromolecule | Name: MAGNESIUM ION / type: ligand / ID: 3 / Number of copies: 29 / Formula: MG |
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Molecular weight | Theoretical: 24.305 Da |
-Macromolecule #4: POTASSIUM ION
Macromolecule | Name: POTASSIUM ION / type: ligand / ID: 4 / Number of copies: 4 / Formula: K |
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Molecular weight | Theoretical: 39.098 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 |
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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: 58.0 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 |