2MMP
Solution structure of a ribosomal protein
Summary for 2MMP
| Entry DOI | 10.2210/pdb2mmp/pdb |
| NMR Information | BMRB: 19860 |
| Descriptor | Uncharacterized protein (1 entity in total) |
| Functional Keywords | ribosomal protein |
| Biological source | Sulfolobus solfataricus |
| Total number of polymer chains | 1 |
| Total formula weight | 9223.80 |
| Authors | Feng, Y. (deposition date: 2014-03-17, release date: 2014-06-11, Last modification date: 2024-05-15) |
| Primary citation | Feng, Y.,Song, X.,Lin, J.,Xuan, J.,Cui, Q.,Wang, J. Structure determination of archaea-specific ribosomal protein L46a reveals a novel protein fold. Biochem.Biophys.Res.Commun., 450:67-72, 2014 Cited by PubMed Abstract: Three archaea-specific ribosomal proteins recently identified show no sequence homology with other known proteins. Here we determined the structure of L46a, the most conserved one among the three proteins, from Sulfolobus solfataricus P2 using NMR spectroscopy. The structure presents a twisted β-sheet formed by the N-terminal part and two helices at the C-terminus. The L46a structure has a positively charged surface which is conserved in the L46a protein family and is the potential rRNA-binding site. Searching homologous structures in Protein Data Bank revealed that the structure of L46a represents a novel protein fold. The backbone dynamics identified by NMR relaxation experiments reveal significant flexibility at the rRNA binding surface. The potential position of L46a on the ribosome was proposed by fitting the structure into a previous electron microscopy map of the ribosomal 50S subunit, which indicated that L46a contacts to domain I of 23S rRNA near a multifunctional ribosomal protein L7ae. PubMed: 24875358DOI: 10.1016/j.bbrc.2014.05.077 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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