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Yorodumi- EMDB-8932: Cryo-EM Structure of Mycobacterium smegmatis 70S C(minus) ribosom... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-8932 | ||||||||||||
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Title | Cryo-EM Structure of Mycobacterium smegmatis 70S C(minus) ribosome 70S-MPY complex | ||||||||||||
Map data | Cryo-EM structure of Mycobacterium smegmatis Cminus ribosome 70S-MPY complex | ||||||||||||
Sample |
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Keywords | Hibernation factor complex / RIBOSOME | ||||||||||||
Function / homology | Function and homology information small ribosomal subunit rRNA binding / large ribosomal subunit / regulation of translation / large ribosomal subunit rRNA binding / 5S rRNA binding / transferase activity / small ribosomal subunit / ribosomal large subunit assembly / cytosolic large ribosomal subunit / tRNA binding ...small ribosomal subunit rRNA binding / large ribosomal subunit / regulation of translation / large ribosomal subunit rRNA binding / 5S rRNA binding / transferase activity / small ribosomal subunit / ribosomal large subunit assembly / cytosolic large ribosomal subunit / tRNA binding / rRNA binding / ribosome / structural constituent of ribosome / translation / ribonucleoprotein complex / mRNA binding / cytosol / cytoplasm Similarity search - Function | ||||||||||||
Biological species | Mycobacterium smegmatis str. MC2 155 (bacteria) / Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155) (bacteria) / Mycobacterium smegmatis (bacteria) | ||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.46 Å | ||||||||||||
Authors | Li Y / Sharma MR / Koripella RK / Yang Y / Kaushal PS / Lin Q / Wade JT / Gray TA / Derbyshire KM / Agrawal RK / Ojha AK | ||||||||||||
Funding support | United States, 3 items
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Citation | Journal: Proc Natl Acad Sci U S A / Year: 2018 Title: Zinc depletion induces ribosome hibernation in mycobacteria. Authors: Yunlong Li / Manjuli R Sharma / Ravi K Koripella / Yong Yang / Prem S Kaushal / Qishan Lin / Joseph T Wade / Todd A Gray / Keith M Derbyshire / Rajendra K Agrawal / Anil K Ojha / Abstract: Bacteria respond to zinc starvation by replacing ribosomal proteins that have the zinc-binding CXXC motif (C+) with their zinc-free (C-) paralogues. Consequences of this process beyond zinc ...Bacteria respond to zinc starvation by replacing ribosomal proteins that have the zinc-binding CXXC motif (C+) with their zinc-free (C-) paralogues. Consequences of this process beyond zinc homeostasis are unknown. Here, we show that the C- ribosome in is the exclusive target of a bacterial protein Y homolog, referred to as mycobacterial-specific protein Y (MPY), which binds to the decoding region of the 30S subunit, thereby inactivating the ribosome. MPY binding is dependent on another mycobacterial protein, MPY recruitment factor (MRF), which is induced on zinc depletion, and interacts with C- ribosomes. MPY binding confers structural stability to C- ribosomes, promoting survival of growth-arrested cells under zinc-limiting conditions. Binding of MPY also has direct influence on the dynamics of aminoglycoside-binding pockets of the C- ribosome to inhibit binding of these antibiotics. Together, our data suggest that zinc limitation leads to ribosome hibernation and aminoglycoside resistance in mycobacteria. Furthermore, our observation of the expression of the proteins of C- ribosomes in in a mouse model of infection suggests that ribosome hibernation could be relevant in our understanding of persistence and drug tolerance of the pathogen encountered during chemotherapy of TB. | ||||||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | EM map: SurfViewMolmilJmol/JSmol |
Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_8932.map.gz | 38.2 MB | EMDB map data format | |
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Header (meta data) | emd-8932-v30.xml emd-8932.xml | 74.8 KB 74.8 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_8932_fsc.xml | 15.8 KB | Display | FSC data file |
Images | emd_8932.png | 225.9 KB | ||
Filedesc metadata | emd-8932.cif.gz | 13.9 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-8932 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-8932 | HTTPS FTP |
-Validation report
Summary document | emd_8932_validation.pdf.gz | 459.4 KB | Display | EMDB validaton report |
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Full document | emd_8932_full_validation.pdf.gz | 458.9 KB | Display | |
Data in XML | emd_8932_validation.xml.gz | 15 KB | Display | |
Data in CIF | emd_8932_validation.cif.gz | 20.5 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-8932 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-8932 | HTTPS FTP |
-Related structure data
Related structure data | 6dziMC 8934C 8937C 6dzkC 6dzpC C: citing same article (ref.) M: atomic model generated by this map |
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Similar structure data |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_8932.map.gz / Format: CCP4 / Size: 357 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | Cryo-EM structure of Mycobacterium smegmatis Cminus ribosome 70S-MPY complex | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.07 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Sample components
+Entire : 70S-MPY complex
+Supramolecule #1: 70S-MPY complex
+Macromolecule #1: 16S rRNA
+Macromolecule #23: 23 S rRNA (3119-MER)
+Macromolecule #24: 5S RNA (118-MER)
+Macromolecule #2: CONSERVED PROTEIN DOMAIN
+Macromolecule #3: 30S ribosomal protein S3
+Macromolecule #4: 30S ribosomal protein S4
+Macromolecule #5: 30S ribosomal protein S5
+Macromolecule #6: 30S ribosomal protein S6
+Macromolecule #7: 30S ribosomal protein S7
+Macromolecule #8: 30S ribosomal protein S8
+Macromolecule #9: 30S ribosomal protein S9
+Macromolecule #10: 30S ribosomal protein S10
+Macromolecule #11: 30S ribosomal protein S11
+Macromolecule #12: 30S ribosomal protein S12
+Macromolecule #13: 30S ribosomal protein S13
+Macromolecule #14: 30S ribosomal protein S15
+Macromolecule #15: 30S ribosomal protein S16
+Macromolecule #16: 30S ribosomal protein S17
+Macromolecule #17: 30S ribosomal protein S19
+Macromolecule #18: 30S ribosomal protein S20
+Macromolecule #19: 30S ribosomal protein S2
+Macromolecule #20: 30S ribosomal protein S18 1
+Macromolecule #21: Ribosome hibernation promoting factor
+Macromolecule #22: 30S ribosomal protein S14
+Macromolecule #25: 50S ribosomal protein L2
+Macromolecule #26: 50S ribosomal protein L3
+Macromolecule #27: 50S ribosomal protein L4
+Macromolecule #28: 50S ribosomal protein L5
+Macromolecule #29: 50S ribosomal protein L6
+Macromolecule #30: 50S ribosomal protein L9
+Macromolecule #31: 50S ribosomal protein L10
+Macromolecule #32: 50S ribosomal protein L11
+Macromolecule #33: 50S ribosomal protein L13
+Macromolecule #34: 50S ribosomal protein L14
+Macromolecule #35: 50S ribosomal protein L15
+Macromolecule #36: 50S ribosomal protein L16
+Macromolecule #37: 50S ribosomal protein L17
+Macromolecule #38: 50S ribosomal protein L18
+Macromolecule #39: 50S ribosomal protein L19
+Macromolecule #40: 50S ribosomal protein L20
+Macromolecule #41: 50S ribosomal protein L21
+Macromolecule #42: 50S ribosomal protein L22
+Macromolecule #43: 50S ribosomal protein L23
+Macromolecule #44: 50S ribosomal protein L24
+Macromolecule #45: 50S ribosomal protein L25
+Macromolecule #46: 50S ribosomal protein L27
+Macromolecule #47: 50S ribosomal protein L29
+Macromolecule #48: 50S ribosomal protein L30
+Macromolecule #49: 50S ribosomal protein L32
+Macromolecule #50: 50S ribosomal protein L33 2
+Macromolecule #51: 50S ribosomal protein L34
+Macromolecule #52: 50S ribosomal protein L35
+Macromolecule #53: 50S ribosomal protein L36
+Macromolecule #54: 50S ribosomal protein L31
+Macromolecule #55: 50S ribosomal protein L28
+Macromolecule #56: Uncharacterized 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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Grid | Model: Quantifoil R1.2/1.3 / Material: COPPER / Support film - Material: CARBON / Support film - topology: CONTINUOUS / Pretreatment - Type: GLOW DISCHARGE |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Instrument: FEI VITROBOT MARK I |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 67.1 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: OTHER / Imaging mode: BRIGHT FIELD |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
+Image processing
-Atomic model buiding 1
Refinement | Space: REAL / Protocol: FLEXIBLE FIT |
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Output model | PDB-6dzi: |