+
Open data
-
Basic information
Entry | ![]() | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Title | EF-G2 bound 70S ribosome complex of M. smegmatis | ||||||||||||
![]() | |||||||||||||
![]() |
| ||||||||||||
![]() | Mycobacterium 70S ribosome / stationary phase / elongation factor G2 / non-canonical factor / RIBOSOME | ||||||||||||
Function / homology | ![]() ribosome disassembly / translation elongation factor activity / large ribosomal subunit / transferase activity / ribosomal small subunit biogenesis / ribosomal small subunit assembly / small ribosomal subunit / 5S rRNA binding / small ribosomal subunit rRNA binding / ribosomal large subunit assembly ...ribosome disassembly / translation elongation factor activity / large ribosomal subunit / transferase activity / ribosomal small subunit biogenesis / ribosomal small subunit assembly / small ribosomal subunit / 5S rRNA binding / small ribosomal subunit rRNA binding / ribosomal large subunit assembly / cytosolic small ribosomal subunit / large ribosomal subunit rRNA binding / cytosolic large ribosomal subunit / cytoplasmic translation / tRNA binding / negative regulation of translation / rRNA binding / structural constituent of ribosome / ribosome / translation / ribonucleoprotein complex / mRNA binding / GTPase activity / GTP binding / RNA binding / zinc ion binding / metal ion binding / cytosol / cytoplasm Similarity search - Function | ||||||||||||
Biological species | ![]() | ||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 4.7 Å | ||||||||||||
![]() | Sengupta J / Baid P | ||||||||||||
Funding support | ![]()
| ||||||||||||
![]() | ![]() Title: Cryo-EM structural analyses reveal a unique role for elongation factor G2 (EF-G2) in Mycobacteria. Authors: Priya Baid / Jayati Sengupta / ![]() Abstract: The gene-encoding translation elongation factor G (EF-G) has undergone gene duplication across various bacterial species including Mycobacteria, and in mammalian mitochondria, leading to the ...The gene-encoding translation elongation factor G (EF-G) has undergone gene duplication across various bacterial species including Mycobacteria, and in mammalian mitochondria, leading to the emergence of the paralogue elongation factor G2 (EF-G2). Our study reveals that mycobacterial EF-G2, unlike EF-G1, neither participates in ribosome-recycling nor significantly contributes to overall translation, suggesting that it plays an alternative role in Mycobacteria. Remarkably, our investigation found a significant overexpression of mycobacterial EF-G2 during the stationary growth phase. Moreover, EF-G2 lacks ribosome-dependent GTPase activity, an observation consistent with previous reports. Cryo-EM analysis of the M. smegmatis 70S ribosome purified from the nutrient-starved (stationary) phase and complexed with EF-G2 unveiled the structural basis for its inability to hydrolyse GTP in a ribosome-dependent manner. Furthermore, we report an unprecedented binding mode of two EF-G2 copies on the 50S ribosomal subunit that impedes subunit association, thereby preventing the formation of active 70S ribosomes. Thus, instead of performing canonical functions, mycobacterial EF-G2 acts as a translation repressor during nutrient starvation. Altogether, our findings shed light on the multifaceted mechanisms by which EF-G2 modulates protein synthesis under nutrient-limited conditions, providing insights into adaptive strategies employed by Mycobacteria to survive in hostile environments. | ||||||||||||
History |
|
-
Structure visualization
-
Downloads & links
-EMDB archive
Map data | ![]() | 129 MB | ![]() | |
---|---|---|---|---|
Header (meta data) | ![]() ![]() | 77 KB 77 KB | Display Display | ![]() |
Images | ![]() | 110.7 KB | ||
Filedesc metadata | ![]() | 15.1 KB | ||
Others | ![]() ![]() | 129.4 MB 129.4 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 978.2 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 977.8 KB | Display | |
Data in XML | ![]() | 14.8 KB | Display | |
Data in CIF | ![]() | 17.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9k0zMC ![]() 9k10C M: atomic model generated by this map C: citing same article ( |
---|---|
Similar structure data | Similarity search - Function & homology ![]() |
-
Links
EMDB pages | ![]() ![]() |
---|---|
Related items in Molecule of the Month |
-
Map
File | ![]() | ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Voxel size | X=Y=Z: 1.38 Å | ||||||||||||||||||||
Density |
| ||||||||||||||||||||
Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
|
-Supplemental data
-
Sample components
+Entire : EF-G2 bound 70S ribosome complex of M. smegmatis
+Supramolecule #1: EF-G2 bound 70S ribosome complex of M. smegmatis
+Macromolecule #1: P/P-site Phe-tRNA(Phe)
+Macromolecule #3: mRNA fragment
+Macromolecule #6: 16S ribosomal RNA
+Macromolecule #7: 5S ribosomal RNA
+Macromolecule #58: 23S ribosomal RNA
+Macromolecule #2: 50S ribosomal protein bL37
+Macromolecule #4: Large ribosomal subunit protein bL12
+Macromolecule #5: Translation elongation factor EF-G
+Macromolecule #8: Small ribosomal subunit protein uS3
+Macromolecule #9: Small ribosomal subunit protein uS4
+Macromolecule #10: Small ribosomal subunit protein uS5
+Macromolecule #11: Small ribosomal subunit protein bS6
+Macromolecule #12: Small ribosomal subunit protein uS7
+Macromolecule #13: Small ribosomal subunit protein uS8
+Macromolecule #14: Small ribosomal subunit protein uS9
+Macromolecule #15: Small ribosomal subunit protein uS10
+Macromolecule #16: Small ribosomal subunit protein uS11
+Macromolecule #17: Small ribosomal subunit protein uS12
+Macromolecule #18: Small ribosomal subunit protein uS13
+Macromolecule #19: Small ribosomal subunit protein uS14B
+Macromolecule #20: Small ribosomal subunit protein uS15
+Macromolecule #21: Small ribosomal subunit protein bS16
+Macromolecule #22: Small ribosomal subunit protein uS17
+Macromolecule #23: Small ribosomal subunit protein bS18B
+Macromolecule #24: Small ribosomal subunit protein uS19
+Macromolecule #25: Small ribosomal subunit protein bS20
+Macromolecule #26: Large ribosomal subunit protein uL23
+Macromolecule #27: Small ribosomal subunit protein uS2
+Macromolecule #28: Large ribosomal subunit protein bL25
+Macromolecule #29: Large ribosomal subunit protein bL27
+Macromolecule #30: Large ribosomal subunit protein bL28
+Macromolecule #31: Large ribosomal subunit protein uL29
+Macromolecule #32: Large ribosomal subunit protein uL30
+Macromolecule #33: Large ribosomal subunit protein bL32
+Macromolecule #34: Large ribosomal subunit protein bL33A
+Macromolecule #35: Large ribosomal subunit protein bL34
+Macromolecule #36: Large ribosomal subunit protein bL35
+Macromolecule #37: 50S ribosomal protein L36
+Macromolecule #38: Large ribosomal subunit protein bL31
+Macromolecule #39: Large ribosomal subunit protein uL2
+Macromolecule #40: Large ribosomal subunit protein uL3
+Macromolecule #41: Large ribosomal subunit protein uL4
+Macromolecule #42: Large ribosomal subunit protein uL5
+Macromolecule #43: Large ribosomal subunit protein uL6
+Macromolecule #44: 50S ribosomal protein L9
+Macromolecule #45: Large ribosomal subunit protein uL10
+Macromolecule #46: Large ribosomal subunit protein uL11
+Macromolecule #47: Large ribosomal subunit protein uL13
+Macromolecule #48: 50S ribosomal protein L14
+Macromolecule #49: Large ribosomal subunit protein uL15
+Macromolecule #50: Large ribosomal subunit protein uL16
+Macromolecule #51: Large ribosomal subunit protein bL17
+Macromolecule #52: Large ribosomal subunit protein uL18
+Macromolecule #53: 50S ribosomal protein L19
+Macromolecule #54: Large ribosomal subunit protein bL20
+Macromolecule #55: Large ribosomal subunit protein bL21
+Macromolecule #56: Large ribosomal subunit protein uL22
+Macromolecule #57: Large ribosomal subunit protein uL24
+Macromolecule #59: PHENYLALANINE
+Macromolecule #60: PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER
+Macromolecule #61: MAGNESIUM ION
+Macromolecule #62: ZINC ION
-Experimental details
-Structure determination
Method | cryo EM |
---|---|
![]() | single particle reconstruction |
Aggregation state | particle |
-
Sample preparation
Buffer | pH: 7.8 |
---|---|
Grid | Model: Quantifoil R2/2 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY ARRAY / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 30 sec. |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Instrument: FEI VITROBOT MARK IV |
-
Electron microscopy
Microscope | TFS KRIOS |
---|---|
Image recording | Film or detector model: FEI FALCON III (4k x 4k) / Average electron dose: 54.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 3.3000000000000003 µm / Nominal defocus min: 1.8 µm |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |