3DD6

Crystal structure of Rph, an exoribonuclease from Bacillus anthracis at 1.7 A resolution

3DD6 の概要

• エントリーDOI: 10.2210/pdb3dd6/pdb
• 分子名称: Ribonuclease PH, SULFATE ION (3 entities in total)
• 機能のキーワード: exoribonuclease, bacillus anthracis, trna maturation, rnase ph., transferase, structural genomics, structural proteomics in europe 2, spine-2
• 由来する生物種: Bacillus anthracis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 28687.41

構造登録者

Rawlings, A.E.,Blagova, E.V.,Levdikov, V.M.,Fogg, M.J.,Wilson, K.S.,Wilkinson, A.J.,Structural Proteomics in Europe 2 (SPINE-2) (登録日: 2008-06-05, 公開日: 2009-02-10, 最終更新日: 2023-08-30)

主引用文献

Rawlings, A.E.,Blagova, E.V.,Levdikov, V.M.,Fogg, M.J.,Wilson, K.S.,Wilkinson, A.J.
The structure of Rph, an exoribonuclease from Bacillus anthracis, at 1.7 A resolution.
Acta Crystallogr.,Sect.F, 65:2-7, 2009

PubMed Abstract: Maturation of tRNA precursors into functional tRNA molecules requires trimming of the primary transcript at both the 5' and 3' ends. Cleavage of nucleotides from the 3' stem of tRNA precursors, releasing nucleotide diphosphates, is accomplished in Bacillus by a phosphate-dependent exoribonuclease, Rph. The crystal structure of this enzyme from B. anthracis has been solved by molecular replacement to a resolution of 1.7 A and refined to an R factor of 19.3%. There is one molecule in the asymmetric unit; the crystal packing reveals the assembly of the protein into a hexamer arranged as a trimer of dimers. The structure shows two sulfate ions bound in the active-site pocket, probably mimicking the phosphate substrate and the phosphate of the 3'-terminal nucleotide of the tRNA precursor. Three other bound sulfate ions point to likely RNA-binding sites.

PubMed: 19153445
DOI: 10.1107/S1744309108041511

実験手法

X-RAY DIFFRACTION (1.702 Å)