5IE8
The pyrazinoic acid binding domain of Ribosomal Protein S1 from Mycobacterium tuberculosis
Summary for 5IE8
| Entry DOI | 10.2210/pdb5ie8/pdb |
| NMR Information | BMRB: 26725 |
| Descriptor | 30S ribosomal protein S1 (1 entity in total) |
| Functional Keywords | tuberculosis, mtrpsa, trans-translation, poa, translation |
| Biological source | Mycobacterium leprae (strain TN) |
| Total number of polymer chains | 1 |
| Total formula weight | 9992.36 |
| Authors | |
| Primary citation | Huang, B.,Fu, J.,Guo, C.,Wu, X.,Lin, D.,Liao, X. (1)H, (15)N, (13)C resonance assignments for pyrazinoic acid binding domain of ribosomal protein S1 from Mycobacterium tuberculosis Biomol NMR Assign, 10:321-324, 2016 Cited by PubMed Abstract: Ribosomal protein S1 of Mycobacterium tuberculosis (MtRpsA) binds to ribosome and mRNA, and plays significant role in the regulation of translation initiation, conventional protein synthesis and transfer-messenger RNA (tmRNA) mediated trans-translation. It has been identified as the target of pyrazinoic acid (POA), a bactericidal moiety from hydrolysis of pyrazinamide, which is a mainstay of combination therapy for tuberculosis. POA prevented the interactions between the C-terminal S1 domain of MtRpsA (residues 280-368, MtRpsA(CTD)_S1) and tmRNA; so that POA can inhibit the trans-translation, which is a key component of multiple quality control pathways in bacteria. However, the details of molecular mechanism and dynamic characteristics for MtRpsA(CTD)_S1 interactions with POA, tmRNA or mRNA are still unclear. Here we present the (1)H, (15)N, (13)C resonance assignments of MtRpsA(CTD)_S1 as well as the secondary structure information based on backbone chemical shifts, which lay foundation for further solution structure determination, dynamic properties characterization and interactions investigation between MtRpsA(CTD)_S1 and tmRNA, RNA or POA. PubMed: 27412769DOI: 10.1007/s12104-016-9692-9 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
