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3NGY

Crystal structure of RNase T (E92G mutant)

Summary for 3NGY
Entry DOI10.2210/pdb3ngy/pdb
Related3NGZ 3NH0 3NH1 3NH2
DescriptorRibonuclease T, his tag sequence, COBALT (II) ION, ... (4 entities in total)
Functional Keywordsexoribonuclease, rna processing, rna maturation, protein-dna interactions, exo-nuclease, hydrolase
Biological sourceEscherichia coli
More
Total number of polymer chains5
Total formula weight103560.52
Authors
Hsiao, Y.-Y.,Yuan, H.S. (deposition date: 2010-06-14, release date: 2011-02-16, Last modification date: 2024-11-06)
Primary citationHsiao, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.204 Å)
Structure validation

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건을2024-11-06부터공개중

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