7KWG
Staphylococcus aureus 30S ribosomal subunit in presence of spermidine
Summary for 7KWG
| Entry DOI | 10.2210/pdb7kwg/pdb |
| EMDB information | 23052 |
| Descriptor | mRNA, 30S ribosomal protein S9, 30S ribosomal protein S10, ... (21 entities in total) |
| Functional Keywords | pathogen, small ribosomal subunit, spermidine, ribosome |
| Biological source | Staphylococcus aureus subsp. aureus NCTC 8325 More |
| Total number of polymer chains | 21 |
| Total formula weight | 788854.46 |
| Authors | Belinite, M.,Khusainov, I.,Marzi, S.,Romby, P.,Yusupov, M.,Hashem, Y. (deposition date: 2020-11-30, release date: 2021-01-27, Last modification date: 2024-05-29) |
| Primary citation | Belinite, M.,Khusainov, I.,Soufari, H.,Marzi, S.,Romby, P.,Yusupov, M.,Hashem, Y. Stabilization of Ribosomal RNA of the Small Subunit by Spermidine in Staphylococcus aureus . Front Mol Biosci, 8:738752-738752, 2021 Cited by PubMed Abstract: Cryo-electron microscopy is now used as a method of choice in structural biology for studying protein synthesis, a process mediated by the ribosome machinery. In order to achieve high-resolution structures using this approach, one needs to obtain homogeneous and stable samples, which requires optimization of ribosome purification in a species-dependent manner. This is especially critical for the bacterial small ribosomal subunit that tends to be unstable in the absence of ligands. Here, we report a protocol for purification of stable 30 S from the Gram-positive bacterium and its cryo-EM structures: in presence of spermidine at a resolution ranging between 3.4 and 3.6 Å and in its absence at 5.3 Å. Using biochemical characterization and cryo-EM, we demonstrate the importance of spermidine for stabilization of the 30 S preserving favorable conformation of the helix 44. PubMed: 34869582DOI: 10.3389/fmolb.2021.738752 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.75 Å) |
Structure validation
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