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Yorodumi- EMDB-63834: Cryo-EM structure of spMETTL16 in complex with U6 snRNA and SAM -
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Open data
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Basic information
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| Title | Cryo-EM structure of spMETTL16 in complex with U6 snRNA and SAM | |||||||||
Map data | Processed by deepEMhancer | |||||||||
Sample |
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Keywords | m6A methyltransferase / U6 snRNA / protein-RNA complex / splicing / TRANSFERASE / TRANSFERASE-RNA complex | |||||||||
| Function / homology | Function and homology informationsnRNA (adenine-N6)-methylation / U6 snRNA m6A methyltransferase / U6 snRNA (adenine-(43)-N(6))-methyltransferase activity / rRNA base methylation / mRNA splicing, via spliceosome / nucleus / cytosol Similarity search - Function | |||||||||
| Biological species | ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.99 Å | |||||||||
Authors | Ju J / Tomita K | |||||||||
| Funding support | Japan, 1 items
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Citation | Journal: Nat Commun / Year: 2025Title: Structures and mechanisms of U6 snRNA mA modification by METTL16. Authors: Jue Ju / Kozo Tomita / ![]() Abstract: The N-methyladenosine (mA) modification in U6 snRNA, catalyzed by METTL16 using S-adenosylmethionine (SAM) as the methyl donor, is required for efficient and accurate pre-mRNA splicing. However, the ...The N-methyladenosine (mA) modification in U6 snRNA, catalyzed by METTL16 using S-adenosylmethionine (SAM) as the methyl donor, is required for efficient and accurate pre-mRNA splicing. However, the mechanism by which METTL16 modifies U6 snRNA with mA remains elusive. Here, we present cryo-EM structures of METTL16 in complex with U6 snRNA, providing insights into the METTL16-mediated modification of U6 snRNA with mA. The structures reveal that U6 snRNA is recruited to METTL16 through specific interactions between the C-terminal kinase-associated 1 (KA-1) domain of METTL16 and the internal stem-loop (ISL) of U6 snRNA. Upon SAM binding to the catalytic pocket within the N-terminal methyltransferase domain (MTD), U6 snRNA undergoes a structural rearrangement that positions the target adenine-containing motif at the catalytic site. This conformational change is followed by an additional structural adjustment of U6 snRNA into a productive conformation, bringing the target adenosine closer to SAM within the catalytic pocket and thereby ensuring efficient mA modification. The KA-1 domain functions as a scaffold for initial substrate recognition and facilitates the subsequent dynamic methylation process within the MTD, highlighting the cooperative roles of METTL16 domains for U6 snRNA modification. | |||||||||
| History |
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_63834.map.gz | 115.2 MB | EMDB map data format | |
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| Header (meta data) | emd-63834-v30.xml emd-63834.xml | 21.5 KB 21.5 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_63834_fsc.xml | 10.7 KB | Display | FSC data file |
| Images | emd_63834.png | 85.4 KB | ||
| Masks | emd_63834_msk_1.map | 129.7 MB | Mask map | |
| Filedesc metadata | emd-63834.cif.gz | 7 KB | ||
| Others | emd_63834_half_map_1.map.gz emd_63834_half_map_2.map.gz | 120.3 MB 120.3 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-63834 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-63834 | HTTPS FTP |
-Validation report
| Summary document | emd_63834_validation.pdf.gz | 596 KB | Display | EMDB validaton report |
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| Full document | emd_63834_full_validation.pdf.gz | 595.6 KB | Display | |
| Data in XML | emd_63834_validation.xml.gz | 19 KB | Display | |
| Data in CIF | emd_63834_validation.cif.gz | 24.8 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-63834 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-63834 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9u48MC ![]() 9m86C ![]() 9u47C 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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Map
| File | Download / File: emd_63834.map.gz / Format: CCP4 / Size: 129.7 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | Processed by deepEMhancer | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.83 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Mask #1
| File | emd_63834_msk_1.map | ||||||||||||
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| Density Histograms |
-Half map: #2
| File | emd_63834_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #1
| File | emd_63834_half_map_2.map | ||||||||||||
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Sample components
-Entire : Schizosaccharomyces pombe N6-methyladenosine methyltransferase ME...
| Entire | Name: Schizosaccharomyces pombe N6-methyladenosine methyltransferase METTL16 in complex with U6 snRNA and SAM |
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| Components |
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-Supramolecule #1: Schizosaccharomyces pombe N6-methyladenosine methyltransferase ME...
| Supramolecule | Name: Schizosaccharomyces pombe N6-methyladenosine methyltransferase METTL16 in complex with U6 snRNA and SAM type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2 |
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| Source (natural) | Organism: ![]() |
-Macromolecule #1: U6 small nuclear RNA (adenine-(43)-N(6))-methyltransferase
| Macromolecule | Name: U6 small nuclear RNA (adenine-(43)-N(6))-methyltransferase type: protein_or_peptide / ID: 1 Details: Residues MET A -22 to SER A 0 are expression tags. MET A 1 to PHE A 23 are part of the protein sequence, based on publication (DOI: 10.1038/s41467-021-23457-6). Number of copies: 1 / Enantiomer: LEVO / EC number: U6 snRNA m6A methyltransferase |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 48.442223 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MGSSHHHHHH SSGLVPRGSH MASMTDKTDI INFDSLARDY PDLRSFVKNG RIDFWNEDAI RTLGKAILDR DYSLRVEFPE NRLCPMVPN RATYIRYIHD LLSSTSGQKD KKRIIGLDIG TGASCIYPLL GCRMYSYDFV GTEIDKFSFE TAKSNILQNN M ESQIKIVL ...String: MGSSHHHHHH SSGLVPRGSH MASMTDKTDI INFDSLARDY PDLRSFVKNG RIDFWNEDAI RTLGKAILDR DYSLRVEFPE NRLCPMVPN RATYIRYIHD LLSSTSGQKD KKRIIGLDIG TGASCIYPLL GCRMYSYDFV GTEIDKFSFE TAKSNILQNN M ESQIKIVL RSKQDCLLPD TEGMEEFTFV MCNPPFYEHE EDFINFKQNP PSGVCTGVYH EMVTEGGEVG FANKILTESK KR KGIQWYT CMFGKKSSVP AVVDKLREQN ISNYGIYELA LGKTKRWIIC WSFQAMRPHN ELIRPSSTSL SKYFPHKVLQ NWT LDPELC AQIDDILQKF LDDNKIPWSK KGSVLEISTK SITWSRKARR ISKSQTSVSS LEGQMKCELN VIDNQLQCKW IEGY DYNVY ESFCSALARA LRDNKK UniProtKB: U6 small nuclear RNA (adenine-(43)-N(6))-methyltransferase |
-Macromolecule #2: U6 small nuclear RNA
| Macromolecule | Name: U6 small nuclear RNA / type: rna / ID: 2 / Number of copies: 1 |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 31.863982 KDa |
| Sequence | String: GAUCUUCGGA UCACUUUGGU CAAAUUGAAA CGAUACAGAG AAGAUUAGCA UGGCCCCUGC ACAAGGAUGA CACUGCGACA UUGAGAGAA AACCCAUUUU GENBANK: GENBANK: 3JB9_N |
-Macromolecule #3: S-ADENOSYLMETHIONINE
| Macromolecule | Name: S-ADENOSYLMETHIONINE / type: ligand / ID: 3 / Number of copies: 1 / Formula: SAM |
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| Molecular weight | Theoretical: 398.437 Da |
| Chemical component information | ![]() ChemComp-SAM: |
-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: 7 |
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| Grid | Model: UltrAuFoil R1.2/1.3 / Material: GOLD / Mesh: 300 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Atmosphere: AIR |
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / 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 K3 BIOQUANTUM (6k x 4k) / Digitization - Dimensions - Width: 4092 pixel / Digitization - Dimensions - Height: 5760 pixel / Number grids imaged: 1 / Number real images: 8497 / Average exposure time: 1.0 sec. / 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 / Cs: 2.7 mm / Nominal defocus max: 1.8 µm / Nominal defocus min: 0.8 µm / Nominal magnification: 105000 |
| Sample stage | Cooling holder cryogen: NITROGEN |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
| Initial model | Chain - Source name: AlphaFold / Chain - Initial model type: in silico model |
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| Output model | ![]() PDB-9u48: |
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Keywords
Authors
Japan, 1 items
Citation



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FIELD EMISSION GUN

