5ME0
Structure of the 30S Pre-Initiation Complex 1 (30S IC-1) Stalled by GE81112
Summary for 5ME0
| Entry DOI | 10.2210/pdb5me0/pdb |
| EMDB information | 3494 |
| Descriptor | 16S ribosomal RNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (27 entities in total) |
| Functional Keywords | ribosome, initiation of translation |
| Biological source | Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) More |
| Total number of polymer chains | 26 |
| Total formula weight | 953587.70 |
| Authors | Lopez-Alonso, J.P.,Fabbretti, A.,Kaminishi, T.,Iturrioz, I.,Brandi, L.,Gil Carton, D.,Gualerzi, C.,Fucini, P.,Connell, S. (deposition date: 2016-11-14, release date: 2017-01-11, Last modification date: 2024-04-24) |
| Primary citation | Lopez-Alonso, J.P.,Fabbretti, A.,Kaminishi, T.,Iturrioz, I.,Brandi, L.,Gil-Carton, D.,Gualerzi, C.O.,Fucini, P.,Connell, S.R. Structure of a 30S pre-initiation complex stalled by GE81112 reveals structural parallels in bacterial and eukaryotic protein synthesis initiation pathways. Nucleic Acids Res., 45:2179-2187, 2017 Cited by PubMed Abstract: In bacteria, the start site and the reading frame of the messenger RNA are selected by the small ribosomal subunit (30S) when the start codon, typically an AUG, is decoded in the P-site by the initiator tRNA in a process guided and controlled by three initiation factors. This process can be efficiently inhibited by GE81112, a natural tetrapeptide antibiotic that is highly specific toward bacteria. Here GE81112 was used to stabilize the 30S pre-initiation complex and obtain its structure by cryo-electron microscopy. The results obtained reveal the occurrence of changes in both the ribosome conformation and initiator tRNA position that may play a critical role in controlling translational fidelity. Furthermore, the structure highlights similarities with the early steps of initiation in eukaryotes suggesting that shared structural features guide initiation in all kingdoms of life. PubMed: 27986852DOI: 10.1093/nar/gkw1251 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (13.5 Å) |
Structure validation
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