6NNB
Solution structure of the Tudor domain of PSHCP
Summary for 6NNB
| Entry DOI | 10.2210/pdb6nnb/pdb |
| NMR Information | BMRB: 30559 |
| Descriptor | Prochlorococcus/Synechococcus Hyper Conserved Protein (1 entity in total) |
| Functional Keywords | nmr spectroscopy, cyanobacteria, trna, tudor domains, rna binding protein |
| Biological source | Prochlorococcus marinus (strain MIT 9303) |
| Total number of polymer chains | 1 |
| Total formula weight | 6471.39 |
| Authors | Bauer, K.M.,Pelligrini, M.,Ragusa, M.J. (deposition date: 2019-01-14, release date: 2019-08-21, Last modification date: 2024-05-15) |
| Primary citation | Bauer, K.M.,Dicovitsky, R.,Pellegrini, M.,Zhaxybayeva, O.,Ragusa, M.J. The structure of a highly-conserved picocyanobacterial protein reveals a Tudor domain with an RNA-binding function. J.Biol.Chem., 294:14333-14344, 2019 Cited by PubMed Abstract: Cyanobacteria of the and marine genera are the most abundant photosynthetic microbes in the ocean. Intriguingly, the genomes of these bacteria are strongly divergent even within each genus, both in gene content and at the amino acid level of the encoded proteins. One striking exception to this is a 62-amino-acid protein, termed / yper-onserved rotein (PSHCP). PSHCP is not only found in all sequenced and marine genomes, but it is also nearly 100% identical in its amino acid sequence across all sampled genomes. Such universal distribution and sequence conservation suggest an essential cellular role of PSHCP in these bacteria. However, its function is unknown. Here, we used NMR spectroscopy to determine its structure, finding that 53 of the 62 amino acids in PSHCP form a Tudor domain, whereas the remainder of the protein is disordered. NMR titration experiments revealed that PSHCP has only a weak affinity for DNA, but an 18.5-fold higher affinity for tRNA, hinting at an involvement of PSHCP in translation. Isothermal titration calorimetry experiments further revealed that PSHCP also binds single-stranded, double-stranded, and hairpin RNAs. These results provide the first insight into the structure and function of PSHCP, suggesting that PSHCP appears to be an RNA-binding protein that can recognize a broad array of RNA molecules. PubMed: 31391250DOI: 10.1074/jbc.RA119.007938 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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