3V9S

Crystal structure of RNase T in complex with a product ssDNA (AAC) with one Mg in the active site

3V9S の概要

• エントリーDOI: 10.2210/pdb3v9s/pdb
• 関連するPDBエントリー: 3NGY 3NGZ 3NH0 3NH1 3NH2 3V9U 3V9W 3V9X 3V9Z 3VA0 3VA3
• 分子名称: Ribonuclease T, DNA (5'-D(*TP*TP*AP*CP*AP*AP*C)-3'), MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: dnase/rnase, 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: 4
• 化学式量合計: 55708.44

構造登録者

Hsiao, Y.-Y.,Yuan, H.S. (登録日: 2011-12-28, 公開日: 2012-07-11, 最終更新日: 2023-11-08)

主引用文献

Hsiao, Y.-Y.,Duh, Y.,Chen, Y.P.,Wang, Y.T.,Yuan, H.S.
How an exonuclease decides where to stop in trimming of nucleic acids: crystal structures of RNase T-product complexes
Nucleic Acids Res., 40:8144-8154, 2012

PubMed Abstract: Exonucleases are key enzymes in the maintenance of genome stability, processing of immature RNA precursors and degradation of unnecessary nucleic acids. However, it remains unclear how exonucleases digest nucleic acids to generate correct end products for next-step processing. Here we show how the exonuclease RNase T stops its trimming precisely. The crystal structures of RNase T in complex with a stem-loop DNA, a GG dinucleotide and single-stranded DNA with different 3'-end sequences demonstrate why a duplex with a short 3'-overhang, a dinucleotide and a ssDNA with a 3'-end C cannot be further digested by RNase T. Several hydrophobic residues in RNase T change their conformation upon substrate binding and induce an active or inactive conformation in the active site that construct a precise machine to determine which substrate should be digested based on its sequence, length and structure. These studies thus provide mechanistic insights into how RNase T prevents over digestion of its various substrates, and the results can be extrapolated to the thousands of members of the DEDDh family of exonucleases.

PubMed: 22718982
DOI: 10.1093/nar/gks548

実験手法

X-RAY DIFFRACTION (2.1 Å)