2hx6 | pdb_00002hx6

Solution structure analysis of the phage T4 endoribonuclease RegB

spinqualitylabelsall models 2hx6, 15 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2hx6 is a 1 chain structure with sequence from Enterobacteria phage t4. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: regB, 61.9 (Enterobacteria phage T4) Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed 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. Structural and functional studies of RegB, a new member of a family of sequence-specific ribonucleases involved in mRNA inactivation on the ribosome.,Odaert B, Saida F, Aliprandi P, Durand S, Crechet JB, Guerois R, Laalami S, Uzan M, Bontems F J Biol Chem. 2007 Jan 19;282(3):2019-28. Epub 2006 Oct 17. PMID:17046813 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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