3NH2

Crystal structure of RNase T in complex with a stem DNA with a 3' overhang

3NH2 の概要

• エントリーDOI: 10.2210/pdb3nh2/pdb
• 関連するPDBエントリー: 3NGY 3NGZ 3NH0 3NH1
• 分子名称: Ribonuclease T, 5'-D(P*TP*TP*AP*CP*AP*AP*C)-3' (3 entities in total)
• 機能のキーワード: exoribonuclease, rna processing, rna maturation, protein-dna interactions, protein-dna complex, exo-nuclease, hydrolase-dna complex, hydrolase/dna
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 111201.79

構造登録者

Hsiao, Y.-Y.,Yuan, H.S. (登録日: 2010-06-14, 公開日: 2011-02-16, 最終更新日: 2024-10-30)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.3 Å)