2MFL
Domain 2 of E. coli ribosomal protein S1
Summary for 2MFL
| Entry DOI | 10.2210/pdb2mfl/pdb |
| Related | 2KHI 2KHJ |
| NMR Information | BMRB: 19554 |
| Descriptor | 30S ribosomal protein S1 (1 entity in total) |
| Functional Keywords | s1, ribosome binding, translation initiation, rna binding, ribosomal protein |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 19983.51 |
| Authors | Giraud, P.,Crechet, J.,Bontems, F.,Uzan, M.,Sizun, C. (deposition date: 2013-10-12, release date: 2014-05-21, Last modification date: 2024-05-15) |
| Primary citation | Giraud, P.,Crechet, J.B.,Uzan, M.,Bontems, F.,Sizun, C. Resonance assignment of the ribosome binding domain of E. coli ribosomal protein S1. Biomol.Nmr Assign., 9:107-111, 2015 Cited by PubMed Abstract: Ribosomal protein S1 is an essential actor for protein synthesis in Escherichia coli. It is involved in mRNA recruitment by the 30S ribosomal subunit and recognition of the correct start codon during translation initiation. E. coli S1 is a modular protein that contains six repeats of an S1 motif, which have distinct functions despite structural homology. Whereas the three central repeats have been shown to be involved in mRNA recognition, the two first repeats that constitute the N-terminal domain of S1 are responsible for binding to the 30S subunit. Here we report the almost complete (1)H, (13)C and (15)N resonance assignment of two fragments of the 30S binding region of S1. The first fragment comprises only the first repeat. The second corresponds to the entire ribosome binding domain. Since S1 is absent from all high resolution X-ray structures of prokaryotic ribosomes, these data provide a first step towards atomic level structural characterization of this domain by NMR. Chemical shift analysis of the first repeat provides evidence for structural divergence from the canonical OB-fold of an S1 motif. In contrast the second domain displays the expected topology for an S1 motif, which rationalizes the functional specialization of the two subdomains. PubMed: 24682851DOI: 10.1007/s12104-014-9554-2 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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