3BK2

Crystal Structure Analysis of the RNase J/UMP complex

Summary for 3BK2

• Entry DOI: 10.2210/pdb3bk2/pdb
• Related: 3BK1
• Descriptor: Metal dependent hydrolase, SULFATE ION, ZINC ION, ... (6 entities in total)
• Functional Keywords: rnase j, endoribonuclease, exoribonuclease, metal dependent hydrolase, metallo-beta-lactamase, hydrolase
• Biological source: Thermus thermophilus
• Total number of polymer chains: 1
• Total formula weight: 64133.30

Authors

de la Sierra-Gallay, I.L.,Zig, L.,Putzer, H. (deposition date: 2007-12-05, release date: 2008-01-22, Last modification date: 2024-10-30)

Primary citation

de la Sierra-Gallay, I.L.,Zig, L.,Jamalli, A.,Putzer, H.
Structural insights into the dual activity of RNase J
Nat.Struct.Mol.Biol., 15:206-212, 2008

PubMed Abstract: The maturation and stability of RNA transcripts is controlled by a combination of endo- and exoRNases. RNase J is unique, as it combines an RNase E-like endoribonucleolytic and a 5'-to-3' exoribonucleolytic activity in a single polypeptide. The structural basis for this dual activity is unknown. Here we report the crystal structures of Thermus thermophilus RNase J and its complex with uridine 5'-monophosphate. A binding pocket coordinating the phosphate and base moieties of the nucleotide in the vicinity of the catalytic center provide a rationale for the 5'-monophosphate-dependent 5'-to-3' exoribonucleolytic activity. We show that this dependence is strict; an initial 5'-PPP transcript cannot be degraded exonucleolytically from the 5'-end. Our results suggest that RNase J might switch promptly from endo- to exonucleolytic mode on the same RNA, a property that has important implications for RNA metabolism in numerous prokaryotic organisms and plant organelles containing RNase J orthologs.

PubMed: 18204464
DOI: 10.1038/nsmb.1376

Experimental method

X-RAY DIFFRACTION (2.1 Å)