3NH1

Crystal structure of RNase T in complex with a preferred ssDNA (TAGG) with two Mg in the active site

Summary for 3NH1

• Entry DOI: 10.2210/pdb3nh1/pdb
• Related: 3NGY 3NGZ 3NH0 3NH2
• Descriptor: Ribonuclease T, 5'-D(*TP*TP*AP*TP*AP*GP*G)-3', MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: exoribonuclease, rna processing, rna maturation, protein-dna interactions, protein-dna complex, exo-nuclease, hydrolase-dna complex, hydrolase/dna
• Biological source: Escherichia coli
• Total number of polymer chains: 8
• Total formula weight: 111680.36

Authors

Hsiao, Y.-Y.,Yuan, H.S. (deposition date: 2010-06-14, release date: 2011-02-16, Last modification date: 2023-11-01)

Primary citation

Hsiao, Y.-Y.,Yang, C.-C.,Lin, C.L.,Lin, J.L.J.,Duh, Y.,Yuan, H.S.
Structural basis for RNA trimming by RNase T in stable RNA 3'-end maturation
Nat.Chem.Biol., 7:236-243, 2011

PubMed Abstract: RNA maturation relies on various exonucleases to remove nucleotides successively from the 5' or 3' end of nucleic acids. However, little is known regarding the molecular basis for substrate and cleavage preference of exonucleases. Our biochemical and structural analyses on RNase T-DNA complexes show that the RNase T dimer has an ideal architecture for binding a duplex with a short 3' overhang to produce a digestion product of a duplex with a 2-nucleotide (nt) or 1-nt 3' overhang, depending on the composition of the last base pair in the duplex. A 'C-filter' in RNase T screens out the nucleic acids with 3'-terminal cytosines for hydrolysis by inducing a disruptive conformational change at the active site. Our results reveal the general principles and the working mechanism for the final trimming step made by RNase T in the maturation of stable RNA and pave the way for the understanding of other DEDD family exonucleases.

PubMed: 21317904
DOI: 10.1038/nchembio.524

Experimental method

X-RAY DIFFRACTION (2.107 Å)