2IS3

Crystal Structure of Escherichia coli RNase T

2IS3 の概要

• エントリーDOI: 10.2210/pdb2is3/pdb
• 関連するPDBエントリー: 2F96
• 分子名称: Ribonuclease T, SULFATE ION (2 entities in total)
• 機能のキーワード: rnase, ribonuclease, exoribonuclease, exonuclease, nuclease, hydrolase, stable rna maturation, trna end-turnover
• 由来する生物種: Escherichia coli K12
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 96752.55

構造登録者

Zuo, Y.,Wang, Y.,Malhotra, A. (登録日: 2006-10-16, 公開日: 2007-04-24, 最終更新日: 2024-10-30)

主引用文献

Zuo, Y.,Zheng, H.,Wang, Y.,Chruszcz, M.,Cymborowski, M.,Skarina, T.,Savchenko, A.,Malhotra, A.,Minor, W.
Crystal Structure of RNase T, an Exoribonuclease Involved in tRNA Maturation and End Turnover.
Structure, 15:417-428, 2007

PubMed Abstract: The 3' processing of most bacterial precursor tRNAs involves exonucleolytic trimming to yield a mature CCA end. This step is carried out by RNase T, a member of the large DEDD family of exonucleases. We report the crystal structures of RNase T from Escherichia coli and Pseudomonas aeruginosa, which show that this enzyme adopts an opposing dimeric arrangement, with the catalytic DEDD residues from one monomer closely juxtaposed with a large basic patch on the other monomer. This arrangement suggests that RNase T has to be dimeric for substrate specificity, and agrees very well with prior site-directed mutagenesis studies. The dimeric architecture of RNase T is very similar to the arrangement seen in oligoribonuclease, another bacterial DEDD family exoribonuclease. The catalytic residues in these two enzymes are organized very similarly to the catalytic domain of the third DEDD family exoribonuclease in E. coli, RNase D, which is monomeric.

PubMed: 17437714
DOI: 10.1016/j.str.2007.02.004

実験手法

X-RAY DIFFRACTION (3.1 Å)