4TOI
Crystal structure of E.coli ribosomal protein S2 in complex with N-terminal domain of S1
Summary for 4TOI
| Entry DOI | 10.2210/pdb4toi/pdb |
| Descriptor | 30S ribosomal protein S2,Ribosomal protein S1, ZINC ION (3 entities in total) |
| Functional Keywords | ribosomal protein, complex, translation |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 1 |
| Total formula weight | 35990.19 |
| Authors | Grishkovskaya, I.,Byrgazov, K.,Moll, I.,Djinovic-Carugo, K. (deposition date: 2014-06-05, release date: 2014-12-31, Last modification date: 2023-12-20) |
| Primary citation | Byrgazov, K.,Grishkovskaya, I.,Arenz, S.,Coudevylle, N.,Temmel, H.,Wilson, D.N.,Djinovic-Carugo, K.,Moll, I. Structural basis for the interaction of protein S1 with the Escherichia coli ribosome. Nucleic Acids Res., 43:661-673, 2015 Cited by PubMed Abstract: In Gram-negative bacteria, the multi-domain protein S1 is essential for translation initiation, as it recruits the mRNA and facilitates its localization in the decoding centre. In sharp contrast to its functional importance, S1 is still lacking from the high-resolution structures available for Escherichia coli and Thermus thermophilus ribosomes and thus the molecular mechanism governing the S1-ribosome interaction has still remained elusive. Here, we present the structure of the N-terminal S1 domain D1 when bound to the ribosome at atomic resolution by using a combination of NMR, X-ray crystallography and cryo-electron microscopy. Together with biochemical assays, the structure reveals that S1 is anchored to the ribosome primarily via a stabilizing π-stacking interaction within the short but conserved N-terminal segment that is flexibly connected to domain D1. This interaction is further stabilized by salt bridges involving the zinc binding pocket of protein S2. Overall, this work provides one hitherto enigmatic piece in the 'ribosome puzzle', namely the detailed molecular insight into the topology of the S1-ribosome interface. Moreover, our data suggest novel mechanisms that have the potential to modulate protein synthesis in response to environmental cues by changing the affinity of S1 for the ribosome. PubMed: 25510494DOI: 10.1093/nar/gku1314 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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