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Yorodumi- EMDB-29305: Cryo-EM structure of RNase-treated RESC-A in trypanosomal RNA editing -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-29305 | ||||||||||||
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Title | Cryo-EM structure of RNase-treated RESC-A in trypanosomal RNA editing | ||||||||||||
Map data | |||||||||||||
Sample |
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Keywords | HEAT repeat / trypanosoma / RNA editing substrate binding complex / gRNA / RNA BINDING PROTEIN-RNA complex | ||||||||||||
Function / homology | Function and homology information regulation of mitochondrial mRNA stability / mitochondrial RNA modification / mitochondrial mRNA processing / RNA modification / RNA stabilization / mitochondrial mRNA editing complex / ribonucleoprotein granule / mitochondrial RNA processing / RNA metabolic process / kinetoplast ...regulation of mitochondrial mRNA stability / mitochondrial RNA modification / mitochondrial mRNA processing / RNA modification / RNA stabilization / mitochondrial mRNA editing complex / ribonucleoprotein granule / mitochondrial RNA processing / RNA metabolic process / kinetoplast / RNA processing / mitochondrial matrix / mRNA binding / mitochondrion / RNA binding / cytoplasm Similarity search - Function | ||||||||||||
Biological species | Trypanosoma brucei (eukaryote) | ||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.7 Å | ||||||||||||
Authors | Liu S / Wang H / Li X / Zhang F / Lee JKJ / Li Z / Yu C / Zhao X / Hu JJ / Suematsu T ...Liu S / Wang H / Li X / Zhang F / Lee JKJ / Li Z / Yu C / Zhao X / Hu JJ / Suematsu T / Alvarez-Cabrera AL / Liu Q / Zhang L / Huang L / Aphasizheva I / Aphasizhev R / Zhou ZH | ||||||||||||
Funding support | United States, 3 items
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Citation | Journal: Science / Year: 2023 Title: Structural basis of gRNA stabilization and mRNA recognition in trypanosomal RNA editing. Authors: Shiheng Liu / Hong Wang / Xiaorun Li / Fan Zhang / Jane K J Lee / Zihang Li / Clinton Yu / Jason J Hu / Xiaojing Zhao / Takuma Suematsu / Ana L Alvarez-Cabrera / Qiushi Liu / Liye Zhang / ...Authors: Shiheng Liu / Hong Wang / Xiaorun Li / Fan Zhang / Jane K J Lee / Zihang Li / Clinton Yu / Jason J Hu / Xiaojing Zhao / Takuma Suematsu / Ana L Alvarez-Cabrera / Qiushi Liu / Liye Zhang / Lan Huang / Inna Aphasizheva / Ruslan Aphasizhev / Z Hong Zhou / Abstract: In , the editosome, composed of RNA-editing substrate-binding complex (RESC) and RNA-editing catalytic complex (RECC), orchestrates guide RNA (gRNA)-programmed editing to recode cryptic mitochondrial ...In , the editosome, composed of RNA-editing substrate-binding complex (RESC) and RNA-editing catalytic complex (RECC), orchestrates guide RNA (gRNA)-programmed editing to recode cryptic mitochondrial transcripts into messenger RNAs (mRNAs). The mechanism of information transfer from gRNA to mRNA is unclear owing to a lack of high-resolution structures for these complexes. With cryo-electron microscopy and functional studies, we have captured gRNA-stabilizing RESC-A and gRNA-mRNA-binding RESC-B and RESC-C particles. RESC-A sequesters gRNA termini, thus promoting hairpin formation and blocking mRNA access. The conversion of RESC-A into RESC-B or -C unfolds gRNA and allows mRNA selection. The ensuing gRNA-mRNA duplex protrudes from RESC-B, likely exposing editing sites to RECC-catalyzed cleavage, uridine insertion or deletion, and ligation. Our work reveals a remodeling event facilitating gRNA-mRNA hybridization and assembly of a macromolecular substrate for the editosome's catalytic modality. | ||||||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_29305.map.gz | 59.5 MB | EMDB map data format | |
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Header (meta data) | emd-29305-v30.xml emd-29305.xml | 23.5 KB 23.5 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_29305_fsc.xml | 9.1 KB | Display | FSC data file |
Images | emd_29305.png | 90.3 KB | ||
Filedesc metadata | emd-29305.cif.gz | 8 KB | ||
Others | emd_29305_half_map_1.map.gz emd_29305_half_map_2.map.gz | 49.6 MB 49.6 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-29305 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-29305 | HTTPS FTP |
-Validation report
Summary document | emd_29305_validation.pdf.gz | 903.7 KB | Display | EMDB validaton report |
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Full document | emd_29305_full_validation.pdf.gz | 903.3 KB | Display | |
Data in XML | emd_29305_validation.xml.gz | 15.9 KB | Display | |
Data in CIF | emd_29305_validation.cif.gz | 21.1 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-29305 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-29305 | HTTPS FTP |
-Related structure data
Related structure data | 8fn4MC 8fn6C 8fncC 8fnfC 8fniC 8fnkC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_29305.map.gz / Format: CCP4 / Size: 64 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: 1.062 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
File | emd_29305_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_29305_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
-Entire : RESC5-tagged isolate with RNase treatment
Entire | Name: RESC5-tagged isolate with RNase treatment |
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Components |
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-Supramolecule #1: RESC5-tagged isolate with RNase treatment
Supramolecule | Name: RESC5-tagged isolate with RNase treatment / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all Details: CTS-tagged RESC5 purified from RNase-treated mitochondrial extract by tandem affinity procedure |
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Source (natural) | Organism: Trypanosoma brucei (eukaryote) |
-Macromolecule #1: RNA-editing substrate-binding complex protein 1 (RESC1)
Macromolecule | Name: RNA-editing substrate-binding complex protein 1 (RESC1) type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Trypanosoma brucei (eukaryote) |
Molecular weight | Theoretical: 52.60868 KDa |
Sequence | String: MLRLLRRSIV GSTFNIMVRR QNQGSVSQGA LNMRDQQAAA AENVTPERVW ALWNEGNLFS LSLAQLQGFL SRCGVRTDPA AKKAAVVRQ VEEYLHSKDT TVKGGGQGAA SPQQHQQHGQ QGGYGRWNQA SVMQPETLLD LSQAGFYEGA ANMVPKAFQL L VSDTAPDV ...String: MLRLLRRSIV GSTFNIMVRR QNQGSVSQGA LNMRDQQAAA AENVTPERVW ALWNEGNLFS LSLAQLQGFL SRCGVRTDPA AKKAAVVRQ VEEYLHSKDT TVKGGGQGAA SPQQHQQHGQ QGGYGRWNQA SVMQPETLLD LSQAGFYEGA ANMVPKAFQL L VSDTAPDV VVSRVNTTAF PGFPSNTECY TLGASEKDVA IRSRYSKVLQ WCCLNMSNLQ MDGELYVDFG KLLLKPSVMR KN RRIVSSY TLQQRLQVNH PYTWVPTLPE SCLSKIQEQF LQPEGFAPIG KGVQLTYSGT IKRSKDQLHV DLDNKGKVLA VNS AWVNLQ TAWCTHAKGP DVRLLLRSRP PIRRQDVELF ASTPIIKLAD DDVADVLPPE HGQLVYLSED ETRLFERVSD RGVT ITVRE VKRQPLIILR DEEEDPRVEY SLSAHIPANA AKATDVRAVG LTAFELAGRL AGLVAEDFVR EYGCEAKL UniProtKB: Guide RNA associated protein, GAP2 |
-Macromolecule #2: RNA-editing substrate-binding complex protein 2 (RESC2)
Macromolecule | Name: RNA-editing substrate-binding complex protein 2 (RESC2) type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Trypanosoma brucei (eukaryote) |
Molecular weight | Theoretical: 55.526117 KDa |
Sequence | String: MLRARLKIFS ALNGATSAFS RAVAPLQIAT RQQSFSAAAP AASGDFSHIT RNTVWGLWNE GNLFSLSVPE LAFFLQEHCR VANVDPRAK KSALVRQVEE ILSAEQQASA TVPQEDNPHA IVVTDYDRAE DALEEADEYG DWGAEPGFED RRELDFMELS P GRMGERYD ...String: MLRARLKIFS ALNGATSAFS RAVAPLQIAT RQQSFSAAAP AASGDFSHIT RNTVWGLWNE GNLFSLSVPE LAFFLQEHCR VANVDPRAK KSALVRQVEE ILSAEQQASA TVPQEDNPHA IVVTDYDRAE DALEEADEYG DWGAEPGFED RRELDFMELS P GRMGERYD PLSPRAFQLL HSETATDVGI ASIDPSKLPG QSKVKNALAA IHVAPNDANK MRFRMAFEWC LMNIWNMNMP GE LNIGAGK ALYYRSVAKQ NRNVMPLWTV QKHLYAQHPY AWFAIASESN VAAMESLAAA LNMSIQQERT TSYKVTIRRM AEF FDCELN GQLKCTMMNK PWDRFFVSHY IRSKMPDLRY VVRARHPIKK RIADAYLEAD ILRSTRDSVQ SVLSPELGDV VYCC ERVVR KWAKKTATGV TLQLVETKRT PLIITKAGDE GERLEYEWIV PLPQQAERID IAALTDELWE YGNKLAAALE EGMEE LMVH TMTAVSAY UniProtKB: Mitochondrial guide RNA binding complex subunit 2 |
-Macromolecule #3: RNA-editing substrate-binding complex protein 3 (RESC3)
Macromolecule | Name: RNA-editing substrate-binding complex protein 3 (RESC3) type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Trypanosoma brucei (eukaryote) |
Molecular weight | Theoretical: 53.146617 KDa |
Sequence | String: MSNPFEKVAR GIAFKMRSKV HKQGYSNTVM AQQARRLSPT GLLAMERLTE LTALQQRHQC TFDPALRSKA TQILRTLPLL SIDEDPYFT HTQRALRLAA YFGAVDLPVT YALINQHTKN AFMLDAFSMA SFFYTLAKLK HPQTKEIVGI LLPRLREVAP E LIAREAVH ...String: MSNPFEKVAR GIAFKMRSKV HKQGYSNTVM AQQARRLSPT GLLAMERLTE LTALQQRHQC TFDPALRSKA TQILRTLPLL SIDEDPYFT HTQRALRLAA YFGAVDLPVT YALINQHTKN AFMLDAFSMA SFFYTLAKLK HPQTKEIVGI LLPRLREVAP E LIAREAVH ILRLLCSIQM ADAQLVKVVT ETVVATAADV PLRDARQCAF ILSETFPEEA QRILGAVEHR LCDDIDMNAD AN EVKTTIL DVCRVVSATC KGPRRLLNSV ARRSMELLPQ LTPLDVAFVL KAFHLSSYRH LRLLRVLSSS LAASFPTSNV TKE HGLAAS IVVQSLAHFY LSGCEEVVVT LVNASVNVLE GLNLALTLLA CVRLRCVSPG VDPAVDALCS GAPMRRYVHN AHSM QVTSR ILYGLAHAGR CRSDEEVAIV LPLLKSVVRT PGALRDDCRG FLLDAVTALG ADGECSNDAL QEQVRKVYER LSQDG GK UniProtKB: Mitochondrial RNA binding protein |
-Macromolecule #4: RNA-editing substrate-binding complex protein 4 (RESC4)
Macromolecule | Name: RNA-editing substrate-binding complex protein 4 (RESC4) type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Trypanosoma brucei (eukaryote) |
Molecular weight | Theoretical: 120.847914 KDa |
Sequence | String: MNGRLYCLIR RITSPPVATR LIKEELCLSM AAIARLPLRR DQLAHVTNTE AITTRAQRIS HLCTPTELGM IAEGAEALSC NRFDLADAL IDGAYESVRR AASSTRLSHV SAIARYSASI KTYGNETITT LLKAGASLLQ KNDSVPVLKS FLGVAQSHLT D GEMRVLID ...String: MNGRLYCLIR RITSPPVATR LIKEELCLSM AAIARLPLRR DQLAHVTNTE AITTRAQRIS HLCTPTELGM IAEGAEALSC NRFDLADAL IDGAYESVRR AASSTRLSHV SAIARYSASI KTYGNETITT LLKAGASLLQ KNDSVPVLKS FLGVAQSHLT D GEMRVLID EMCAKATEEQ RLCINSIGTQ SLAKDAAKCG EETLTKGNED GDETAVDDEE TQAWDMLRAR QWMLQLVRCG KP PTAAEAV QAMELYAHFA VRDFVLHEKI EDLVLLVLPT GNKFHLNEMH KIVLRSPNLF PRVRNTLGQD HSGVSDVHRA DRG VEWSDD PASSLTTTYT TSRAYSMLLL GQRLSEDIMF DVVQEQSETI PVDVAAQAAC LFAEKGDIPE GVILRLSAEL EHIS PQGVT AFVRAARRDS SGALLPHYAA VLNRFTERDL CDTPLETLLQ MCEVFALPAP RGTSEGDNDS INESQSKFQK ALIVR LFSV IQGSRDVPFL CKVAKAVRAF DANDELIQFV CSSICAQGAL SECEALIAFD MIRCCDFVYE PLLDAMEPVF RRLVES VSA MLEGKSTIND VEVRRCACFA TLQSEFDCPD FETLASLLVH TVEKNVTGCP VELIPSVGLL CVRTRRTSAL YIVGNKL EG NMQQLSDDAI GELARLLVGT ENLATKELAV EFQSVVVSRL LRQQSLPPDV VALSAVVWLR QGDKVGTIDE RSVDYIIK W MYAIGSSVYT DLCLAVHLSA SVESLSNALI DDLPRRLELL TTNEMANAIF GLGEVSDMGA RLSHQLVAER CSDYVVDHS QEFWSGKVIA RLLYGFSRMH CTKRSLYNVF ATRLAHRPVF SLLDQEAISF AIAAFGRVKY LDKKLFDRFT RWILDHSKDL NAAELLLTI RGVSRVMLLN DQLYDDLGSK AAEKVKEFPI ESQCVLLSSF GSLGVEHERL ASRMVSSIAE NREELTDATK A VDVITSLW SMNYDVEDDK HVAQLADWVV QRAEELTDES IGKLCLVLSD TNWRHVPLVR AIAEQSVRLQ GQQSISPKCC RE VLDVLGT FMIHHQGARE NLSALGRSIS KERIQLSEEE EQHLQLLLRR UniProtKB: Mitochondrial RNA binding complex 1 subunit |
-Macromolecule #5: RNA-editing substrate-binding complex protein 5 (RESC5)
Macromolecule | Name: RNA-editing substrate-binding complex protein 5 (RESC5) type: protein_or_peptide / ID: 5 Details: RESC5 is tagged in situ in Trypanosoma brucei (5691), which shared the same native environment as other RESC proteins. Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Trypanosoma brucei (eukaryote) |
Molecular weight | Theoretical: 43.469484 KDa |
Sequence | String: MLRHTSRNNA LHAFVRSPHY RTIPSAGPNG IVVNRDMLVH QFRDFYKTLQ HCSLVDKVHL MSERPSVEAL RVADQMVSIG ATFLEMPLT GMEHRATEFM ESMRYVRGAG GPSTLASYLQ DTENCRCNSG DVVCLPNGIA VGHGPRTNAV AHTTLKQLFE V KDDQFSFD ...String: MLRHTSRNNA LHAFVRSPHY RTIPSAGPNG IVVNRDMLVH QFRDFYKTLQ HCSLVDKVHL MSERPSVEAL RVADQMVSIG ATFLEMPLT GMEHRATEFM ESMRYVRGAG GPSTLASYLQ DTENCRCNSG DVVCLPNGIA VGHGPRTNAV AHTTLKQLFE V KDDQFSFD VFTLEQEGDA PPLGDYFGFA GSNVLLTWKD EHGLLAVDQY QQKQPHTEMN VVYLEPGCHF LSFYGVDHTI DV LVQKGYE RSMDSIAAAG LNPIPVQWSE MDKLGISMRA AVLPLKFFKA NVGGMLSRNK SRGARWQTHQ LQKGSGSGSA SSG ASAAGS SGASASSGAS AAGSSGASAG HHHHHHHHHH SGSEDQVDPR LIDGKASAWS HPQFEKGGGS GGGSGGSAWS HPQF EK UniProtKB: Mitochondrial RNA binding protein |
-Macromolecule #6: RNA-editing substrate-binding complex protein 6 (RESC6)
Macromolecule | Name: RNA-editing substrate-binding complex protein 6 (RESC6) type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Trypanosoma brucei (eukaryote) |
Molecular weight | Theoretical: 57.823484 KDa |
Sequence | String: MRSALRRCIL RHQGCLRMKQ SLSAFPTVVT GMTRHQGNSL IGTTHGAELS LAGDPQSVSH LSARNIATEA LQMKKLHQER GGNPMLAQQ ARRVLFATSI AGQNLDARSV ALLLNTAVYF GMESDAKLVR ECIDYCLKND KLITVDVLPI VVTACATLKS R DAREVIEM ...String: MRSALRRCIL RHQGCLRMKQ SLSAFPTVVT GMTRHQGNSL IGTTHGAELS LAGDPQSVSH LSARNIATEA LQMKKLHQER GGNPMLAQQ ARRVLFATSI AGQNLDARSV ALLLNTAVYF GMESDAKLVR ECIDYCLKND KLITVDVLPI VVTACATLKS R DAREVIEM QAQKAARNAK FLDAKDVTNI ISAFSKTGIN HEKLFAFLSR RVQTLARVGE FEAAHLVILA NAFSRLRYRD KF LFGAIAR RAMSLRERVT VNELVPLIVA FSKIGLKDPK LSKRFATKAM EYVDQMNAEQ VASMFMAFAY FGIRYDQLFG VLT NRAVEL IDEFNAQYIS TTLNAFQRIG INNPELFDNL AERALAVVQD HDARDISKTV TALAHFGLKD EELFKRLASH AASI ADQFD AMGLVNTAHA FARTNFLQQD MAVALSERSV YVCRLLDAGE TRRLLWALAK FQVRDPKILT PVFNRCLALH YDFFA DPTG SEEIEEIFDF YGPNFCPPLY QLYISRGSTP QA UniProtKB: Guide RNA binding protein |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.5 |
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Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 281.15 K / Instrument: FEI VITROBOT MARK IV |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: SUPER-RESOLUTION / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | C2 aperture diameter: 50.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.5 µm |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |