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- PDB-7qgr: Structure of the SmrB-bound E. coli disome - collided 70S ribosome -
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Open data
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Basic information
Entry | Database: PDB / ID: 7qgr | ||||||
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Title | Structure of the SmrB-bound E. coli disome - collided 70S ribosome | ||||||
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![]() | RIBOSOME / Ribosome rescue / disome / ribosome collision / stalling / no-go complex / nuclease / SmrB | ||||||
Function / homology | ![]() stringent response / mRNA base-pairing translational repressor activity / ornithine decarboxylase inhibitor activity / transcription antitermination factor activity, RNA binding / transcriptional attenuation / endoribonuclease inhibitor activity / RNA-binding transcription regulator activity / negative regulation of cytoplasmic translation / translational termination / four-way junction DNA binding ...stringent response / mRNA base-pairing translational repressor activity / ornithine decarboxylase inhibitor activity / transcription antitermination factor activity, RNA binding / transcriptional attenuation / endoribonuclease inhibitor activity / RNA-binding transcription regulator activity / negative regulation of cytoplasmic translation / translational termination / four-way junction DNA binding / DnaA-L2 complex / translation repressor activity / negative regulation of DNA-templated DNA replication initiation / ribosome assembly / mRNA regulatory element binding translation repressor activity / assembly of large subunit precursor of preribosome / transcription elongation factor complex / DNA endonuclease activity / regulation of DNA-templated transcription elongation / cytosolic ribosome assembly / transcription antitermination / response to reactive oxygen species / DNA-templated transcription termination / response to radiation / ribosomal large subunit assembly / mRNA 5'-UTR binding / large ribosomal subunit / ribosome biogenesis / regulation of translation / ribosomal small subunit biogenesis / ribosomal small subunit assembly / small ribosomal subunit / small ribosomal subunit rRNA binding / transferase activity / 5S rRNA binding / large ribosomal subunit rRNA binding / cytosolic small ribosomal subunit / endonuclease activity / cytosolic large ribosomal subunit / tRNA binding / cytoplasmic translation / rRNA binding / negative regulation of translation / ribosome / structural constituent of ribosome / ribonucleoprotein complex / translation / response to antibiotic / negative regulation of DNA-templated transcription / mRNA binding / DNA binding / RNA binding / zinc ion binding / membrane / metal ion binding / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 5.7 Å | ||||||
![]() | Kratzat, H. / Buschauer, R. / Berninghausen, O. / Beckmann, R. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Ribosome collisions induce mRNA cleavage and ribosome rescue in bacteria. Authors: Kazuki Saito / Hanna Kratzat / Annabelle Campbell / Robert Buschauer / A Maxwell Burroughs / Otto Berninghausen / L Aravind / Rachel Green / Roland Beckmann / Allen R Buskirk / ![]() ![]() Abstract: Ribosome rescue pathways recycle stalled ribosomes and target problematic mRNAs and aborted proteins for degradation. In bacteria, it remains unclear how rescue pathways distinguish ribosomes stalled ...Ribosome rescue pathways recycle stalled ribosomes and target problematic mRNAs and aborted proteins for degradation. In bacteria, it remains unclear how rescue pathways distinguish ribosomes stalled in the middle of a transcript from actively translating ribosomes. Here, using a genetic screen in Escherichia coli, we discovered a new rescue factor that has endonuclease activity. SmrB cleaves mRNAs upstream of stalled ribosomes, allowing the ribosome rescue factor tmRNA (which acts on truncated mRNAs) to rescue upstream ribosomes. SmrB is recruited to ribosomes and is activated by collisions. Cryo-electron microscopy structures of collided disomes from E. coli and Bacillus subtilis show distinct and conserved arrangements of individual ribosomes and the composite SmrB-binding site. These findings reveal the underlying mechanisms by which ribosome collisions trigger ribosome rescue in bacteria. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 3.8 MB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 1.3 MB | Display | ![]() |
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Full document | ![]() | 1.5 MB | Display | |
Data in XML | ![]() | 201.9 KB | Display | |
Data in CIF | ![]() | 330.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 13958MC ![]() 7qg8C ![]() 7qghC ![]() 7qgnC ![]() 7qguC ![]() 7qh4C C: citing same article ( M: map data used to model this data |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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Components
-RNA chain , 6 types, 6 molecules ONMx0u
#1: RNA chain | Mass: 38790.090 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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#30: RNA chain | Mass: 941306.188 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#34: RNA chain | Mass: 24060.287 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#35: RNA chain | Mass: 221443.094 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) ![]() |
#36: RNA chain | Mass: 498725.406 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#58: RNA chain | Mass: 23545.971 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
+50S ribosomal protein ... , 31 types, 31 molecules PQRSTVWXYZabcdefghijklmnopqrLCU
+30S ribosomal protein ... , 21 types, 21 molecules 123456789ABDEFGHIJKst
-Protein , 1 types, 1 molecules v
#59: Protein | Mass: 20841.168 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: yfcN, mutS2, smrB, smrB_1, smrB_2, A5U30_004390, A8499_001840, A9819_13690, A9X72_07680, ABE90_016875, ACN68_23030, ACN81_17810, ACU57_26745, AT845_000599, AWP93_07555, BANRA_00899, BANRA_ ...Gene: yfcN, mutS2, smrB, smrB_1, smrB_2, A5U30_004390, A8499_001840, A9819_13690, A9X72_07680, ABE90_016875, ACN68_23030, ACN81_17810, ACU57_26745, AT845_000599, AWP93_07555, BANRA_00899, BANRA_03120, BANRA_03372, BF481_001004, BG944_000572, BGZ_01188, BGZ_03662, BHS81_14420, BIZ41_10480, BJI68_12470, BK292_05530, BMT49_14945, BN17_16361, BO068_000573, BOB65_001429, BOH76_07895, BON63_04725, BON64_17650, BON65_13895, BON66_23670, BON67_14425, BON68_20955, BON70_19955, BON72_07945, BON73_17545, BON74_06335, BON75_03320, BON76_16635, BON77_02335, BON78_04290, BON79_05115, BON80_19510, BON84_07205, BON88_15485, BON89_17570, BON90_11325, BON93_24455, BON94_16970, BON95_09375, BON97_08585, BON98_08660, BR158_002903, BSR05_08700, BTQ06_04170, BvCmsF30A_00313, BvCmsHHP019_01505, BvCmsHHP019_04741, BvCmsHHP056_04467, BvCmsKKP061_01272, BvCmsKSNP073_04721, BvCmsNSP072_04545, BVL39_15455, C2121_000219, C2U48_22750, C5N07_03940, C5Y87_03970, C9114_16420, C9160_05935, CCS08_07685, CCV12_002627, CDC27_12170, CG692_16040, CG831_000106, CIG67_19185, CQB02_04630, CR538_08010, CT143_04915, CV83915_03834, CWS33_01470, D3G36_02825, D9D77_18555, D9H94_01080, D9J61_20205, DAH18_01290, DAH19_01275, DAH20_01625, DAH22_02175, DAH27_09560, DAH28_11500, DAH29_05910, DAH30_16955, DAH31_06915, DAH32_12865, DAH34_11100, DAH35_01300, DAH36_15590, DAH37_19730, DAH41_07365, DAH50_05250, DEN88_00035, DEN89_08320, DEN90_05265, DEN91_02555, DEN92_02065, DEN93_02685, DEN94_01290, DEN95_01315, DEN96_01750, DEN97_01415, DEN98_01420, DEN99_05995, DEO00_00270, DEO01_17030, DEO02_01830, DEO03_03920, DEO04_00005, DEO05_00005, DEO06_08185, DEO07_00005, DEO08_00005, DEO09_00005, DEO10_00005, DEO11_00005, DEO12_00005, DEO13_01820, DEO14_01755, DEO15_01085, DEO17_01750, DEO18_04800, DEO19_01300, DEO20_01795, DIV22_21330, DN627_21615, DNQ45_19055, DRW19_09740, DS732_17835, DTL90_12855, DTM16_09590, DXT69_04490, DXT70_01870, DXT71_03185, E2112_03655, E2113_09810, E2117_01065, E2119_16395, E2121_01160, E2134_04330, E3N34_02270, E5P23_02715, E5P24_14725, E5P25_01670, E5P30_14800, E5P31_09445, E5P32_05070, E5P33_05410, E5P35_06605, E5P36_01995, E5P37_00385, E5P39_08050, E5P40_09805, E5P41_10890, E5P42_00250, E5P43_12380, E5P44_13535, E5P45_12690, E5P46_02815, E5P47_11675, E5P48_09480, E5P49_00460, E5P50_14395, E5P51_21390, E5S35_19735, E5S36_02955, E5S38_02620, E5S39_01460, E5S42_01695, E5S43_19350, E5S44_00375, E5S45_16565, E5S47_01205, E5S48_14270, E5S51_02300, E5S52_02190, E5S53_18875, E5S55_19065, E5S56_02640, E5S57_06985, EA239_07420, EA435_01595, EAN77_01305, EAX79_20205, EC1094V2_1345, EC3234A_175c01110, EC95NR1_01492, ED648_12345, EHD79_00295, EHH55_04655, EI021_18035, EIZ93_06290, EKI52_23470, ELT16_18350, ELT20_15195, ELT24_01425, ELT26_03990, ELT30_01440, ELT32_01920, ELT34_02590, ELT35_07845, ELT36_06875, ELT39_20410, ELT40_03580, ELT44_07815, ELT45_01435, ELT46_01450, ELT48_05880, ELT54_16840, ELT55_13610, ELT59_03260, ELT60_09215, ELT61_19220, ELT63_16105, ELT72_01435, ELU07_15110, ELU82_03765, ELU88_16655, ELU89_04385, ELU91_15800, ELU94_18550, ELU96_02215, ELU97_18185, ELU98_09905, ELV00_03615, ELV01_12085, ELV03_05730, ELV04_06410, ELV05_03280, ELV07_11430, ELV11_03535, ELV12_11720, ELV13_16905, ELV22_00040, ELV23_22840, ELV24_07090, ELV29_06140, ELX56_00135, ELX68_00090, ELX70_01865, ELX79_14975, ELX83_13520, ELX85_05845, ELY02_00645, ELY05_05535, ELY23_09510, ELY24_08500, ELY31_00705, ELY50_09115, ERS085406_02073, ERS139208_00454, EYV17_01290, EYV18_11375, F0L67_02300, F2N31_09430, F7F11_19875, F9V24_13620, F9X20_21990, FDM60_03010, FE587_23440, FEJ01_05060, FEL34_15690, FOI11_001300, FOI11_18750, FQ007_23030, FQF29_20000, FTV90_21245, FV293_07005, G3565_01615, G9448_22280, GF699_03390, GFY34_16620, GIB53_14855, GKF86_02695, GKF89_15515, GKG12_06190, GNZ05_23665, GP650_07760, GP662_01570, GP711_04770, GP946_05950, GQA06_05730, GQE64_02945, GQM09_01760, GQM13_01410, GQW07_19785, GRC73_01145, GRO95_21555, GRW57_06930, GRW81_01820, GUB92_01975, GUI33_05790, H0O53_19725, H0O72_00040, H6Y26_004289, HI055_002425, HIE29_002473, HIN64_001808, HKA49_003965, HLZ50_13880, HmCms169_00759, HMU06_04960, HMV41_01130, HV109_07165, HV146_16035, HV209_11120, HVV39_03830, HVX32_14355, HVY77_08085, HVZ29_14235, HX136_07310, I6H02_06990, IAI11_22020, IFB95_000286, IH772_06500, J0541_000123, J5U05_001006, JE86ST02C_27550, JE86ST05C_28400, JFD_00470, JNP96_19200, NCTC10089_01526, NCTC10767_02776, NCTC10865_01974, NCTC11181_03768, NCTC13148_02067, NCTC13216_05049, NCTC7928_01110, NCTC8008_00929, NCTC8009_02822, NCTC8179_04654, NCTC8333_01761, NCTC8450_03992, NCTC8621_01639, NCTC8622_03767, NCTC8960_04324, NCTC9001_01891, NCTC9036_01593, NCTC9045_01822, NCTC9073_04248, NCTC9111_01754, NCTC9775_05405, ND22_002524, PGD_00891, RG28_10175, SAMEA3472044_01606, SAMEA3472056_00624, SAMEA3472067_00013, SAMEA3472080_03598, SAMEA3751407_01308, SAMEA3752557_00674, WR15_08435 Production host: ![]() ![]() |
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-Non-polymers , 3 types, 12 molecules ![](data/chem/img/MG.gif)
![](data/chem/img/K.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/K.gif)
![](data/chem/img/HOH.gif)
#60: Chemical | #61: Chemical | ChemComp-K / | #62: Water | ChemComp-HOH / | |
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-Details
Has ligand of interest | N |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
Component | Name: collided ribosome of the SmrB-bound disome structure / Type: RIBOSOME / Entity ID: #1-#59 / Source: NATURAL |
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Molecular weight | Experimental value: NO |
Source (natural) | Organism: ![]() ![]() |
Buffer solution | pH: 7.5 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 3500 nm / Nominal defocus min: 500 nm |
Image recording | Electron dose: 42.4 e/Å2 / Film or detector model: FEI FALCON III (4k x 4k) |
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Processing
CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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3D reconstruction | Resolution: 5.7 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 32412 / Symmetry type: POINT |