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Open data
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Basic information
| Entry | Database: PDB / ID: 8xz3 | |||||||||
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| Title | Mycobacterium smegmatis 50S ribosomal subunit with Erythromycin | |||||||||
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Keywords | RIBOSOME / Antibiotic | |||||||||
| Function / homology | Function and homology informationlarge ribosomal subunit / transferase activity / 5S rRNA binding / ribosomal large subunit assembly / large ribosomal subunit rRNA binding / cytosolic large ribosomal subunit / cytoplasmic translation / tRNA binding / negative regulation of translation / rRNA binding ...large ribosomal subunit / transferase activity / 5S rRNA binding / ribosomal large subunit assembly / 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 / metal ion binding / cytoplasm Similarity search - Function | |||||||||
| Biological species | Mycolicibacterium smegmatis MC2 155 (bacteria) | |||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.6 Å | |||||||||
Authors | Srinivasan, K. / Banerjee, A. / Sengupta, J. | |||||||||
| Funding support | India, 2items
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Citation | Journal: Structure / Year: 2024Title: Cryo-EM structures reveal the molecular mechanism of HflX-mediated erythromycin resistance in mycobacteria. Authors: Krishnamoorthi Srinivasan / Aneek Banerjee / Jayati Sengupta / ![]() Abstract: Mycobacterial HflX confers resistance against macrolide antibiotics. However, the exact molecular mechanism is poorly understood. To gain further insights, we determined the cryo-EM structures of M. ...Mycobacterial HflX confers resistance against macrolide antibiotics. However, the exact molecular mechanism is poorly understood. To gain further insights, we determined the cryo-EM structures of M. smegmatis (Msm) HflX-50S subunit and 50S subunit-erythromycin (ERY) complexes at a global resolution of approximately 3 Å. A conserved nucleotide A2286 at the gate of nascent peptide exit tunnel (NPET) adopts a swayed conformation in HflX-50S complex and interacts with a loop within the linker helical (LH) domain of MsmHflX that contains an additional 9 residues insertion. Interestingly, the swaying of this nucleotide, which is usually found in the non-swayed conformation, is induced by erythromycin binding. Furthermore, we observed that erythromycin decreases HflX's ribosome-dependent GTP hydrolysis, resulting in its enhanced binding and anti-association activity on the 50S subunit. Our findings reveal how mycobacterial HflX senses the presence of macrolides at the peptide tunnel entrance and confers antibiotic resistance in mycobacteria. | |||||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 8xz3.cif.gz | 2.1 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb8xz3.ent.gz | 1.6 MB | Display | PDB format |
| PDBx/mmJSON format | 8xz3.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/xz/8xz3 ftp://data.pdbj.org/pub/pdb/validation_reports/xz/8xz3 | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 38788MC ![]() 8kabC M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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Components
-50S ribosomal protein ... , 5 types, 5 molecules 3HLQf
| #1: Protein/peptide | Mass: 2710.179 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Mycolicibacterium smegmatis MC2 155 (bacteria)References: UniProt: A0QTP4 |
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| #9: Protein | Mass: 15949.253 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Mycolicibacterium smegmatis MC2 155 (bacteria)References: UniProt: A0R7F6 |
| #13: Protein | Mass: 13400.625 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Mycolicibacterium smegmatis MC2 155 (bacteria)References: UniProt: A0QSF9 |
| #18: Protein | Mass: 12892.806 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Mycolicibacterium smegmatis MC2 155 (bacteria)References: UniProt: A0QV42 |
| #33: Protein/peptide | Mass: 4341.277 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Mycolicibacterium smegmatis MC2 155 (bacteria)References: UniProt: A0QSL4 |
-RNA chain , 2 types, 2 molecules AB
| #2: RNA chain | Mass: 1011834.750 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Mycolicibacterium smegmatis MC2 155 (bacteria)References: GenBank: 118168627 |
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| #3: RNA chain | Mass: 38061.816 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Mycolicibacterium smegmatis MC2 155 (bacteria)References: GenBank: 118168627 |
+Large ribosomal subunit protein ... , 27 types, 27 molecules CDEFGIJKMNOPRSTUVWXYZabcdeg
-Non-polymers , 1 types, 1 molecules 
| #35: Chemical | ChemComp-ERY / |
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-Details
| Has ligand of interest | Y |
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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
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| Molecular weight | Experimental value: NO | |||||||||||||||||||||
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| 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: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 3300 nm / Nominal defocus min: 1800 nm |
| Image recording | Electron dose: 28.75 e/Å2 / Film or detector model: FEI FALCON III (4k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||
| 3D reconstruction | Resolution: 3.6 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 43558 / Symmetry type: POINT |
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Mycolicibacterium smegmatis MC2 155 (bacteria)
India, 2items
Citation


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FIELD EMISSION GUN