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3NGZ

Crystal structure of RNase T in complex with a non-preferred ssDNA (GC) with one Mg in the active site

3NGZ の概要
エントリーDOI10.2210/pdb3ngz/pdb
関連するPDBエントリー3NGY 3NH0 3NH1 3NH2
分子名称Ribonuclease T, 5'-D(P*GP*C)-3', MAGNESIUM ION, ... (5 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
タンパク質・核酸の鎖数4
化学式量合計52607.28
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: 2023-11-01)
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
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
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.1 Å)
構造検証レポート
Validation report summary of 3ngz
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-22に公開中

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