2HX6
Solution structure analysis of the phage T4 endoribonuclease RegB
Summary for 2HX6
| Entry DOI | 10.2210/pdb2hx6/pdb |
| Descriptor | Ribonuclease (1 entity in total) |
| Functional Keywords | alpha/beta fold, hydrolase |
| Biological source | Enterobacteria phage T4 |
| Total number of polymer chains | 1 |
| Total formula weight | 17939.55 |
| Authors | Odaert, B.,Saida, F.,Uzan, M.,Bontems, F. (deposition date: 2006-08-02, release date: 2006-10-31, Last modification date: 2024-05-29) |
| Primary citation | Odaert, B.,Saida, F.,Aliprandi, P.,Durand, S.,Crechet, J.B.,Guerois, R.,Laalami, S.,Uzan, M.,Bontems, F. Structural and functional studies of RegB, a new member of a family of sequence-specific ribonucleases involved in mRNA inactivation on the ribosome. J.Biol.Chem., 282:2019-2028, 2007 Cited by PubMed Abstract: The RegB endoribonuclease participates in the bacteriophage T4 life cycle by favoring early messenger RNA breakdown. RegB specifically cleaves GGAG sequences found in intergenic regions, mainly in translation initiation sites. Its activity is very low but can be enhanced up to 100-fold by the ribosomal 30 S subunit or by ribosomal protein S1. RegB has no significant sequence homology to any known protein. Here we used NMR to solve the structure of RegB and map its interactions with two RNA substrates. We also generated a collection of mutants affected in RegB function. Our results show that, despite the absence of any sequence homology, RegB has structural similarities with two Escherichia coli ribonucleases involved in mRNA inactivation on translating ribosomes: YoeB and RelE. Although these ribonucleases have different catalytic sites, we propose that RegB is a new member of the RelE/YoeB structural and functional family of ribonucleases specialized in mRNA inactivation within the ribosome. PubMed: 17046813DOI: 10.1074/jbc.M608271200 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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