1OYP

Crystal Structure of the phosphorolytic exoribonuclease RNase PH from Bacillus subtilis

1OYP の概要

• エントリーDOI: 10.2210/pdb1oyp/pdb
• 関連するPDBエントリー: 1OYR 1OYS
• 分子名称: Ribonuclease PH, SULFATE ION (2 entities in total)
• 機能のキーワード: transferase, trna processing
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 161433.40

構造登録者

Harlow, L.S.,Kadziola, A.,Jensen, K.F.,Larsen, S. (登録日: 2003-04-07, 公開日: 2004-03-09, 最終更新日: 2024-02-14)

主引用文献

Harlow, L.S.,Kadziola, A.,Jensen, K.F.,Larsen, S.
Crystal structure of the phosphorolytic exoribonuclease RNase PH from Bacillus subtilis and implications for its quaternary structure and tRNA binding.
Protein Sci., 13:668-677, 2004

PubMed Abstract: RNase PH is a member of the family of phosphorolytic 3' --> 5' exoribonucleases that also includes polynucleotide phosphorylase (PNPase). RNase PH is involved in the maturation of tRNA precursors and especially important for removal of nucleotide residues near the CCA acceptor end of the mature tRNAs. Wild-type and triple mutant R68Q-R73Q-R76Q RNase PH from Bacillus subtilis have been crystallized and the structures determined by X-ray diffraction to medium resolution. Wild-type and triple mutant RNase PH crystallize as a hexamer and dimer, respectively. The structures contain a rare left-handed beta alpha beta-motif in the N-terminal portion of the protein. This motif has also been identified in other enzymes involved in RNA metabolism. The RNase PH structure and active site can, despite low sequence similarity, be overlayed with the N-terminal core of the structure and active site of Streptomyces antibioticus PNPase. The surface of the RNase PH dimer fit the shape of a tRNA molecule.

PubMed: 14767080
DOI: 10.1110/ps.03477004

実験手法

X-RAY DIFFRACTION (2.76 Å)