1MGR

Crystal structure of RNase Sa3,cytotoxic microbial ribonuclease

1MGR の概要

• エントリーDOI: 10.2210/pdb1mgr/pdb
• 関連するPDBエントリー: 1MGW 1RGG
• 分子名称: Guanyl-specific ribonuclease Sa3, SULFATE ION (3 entities in total)
• 機能のキーワード: alpha/beta protein, ub rolls, hydrolase
• 由来する生物種: Streptomyces aureofaciens
• 細胞内の位置: Secreted: P30289
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11153.19

構造登録者

Sevcik, J.,Urbanikova, L.,Leland, P.A.,Raines, R.T. (登録日: 2002-08-16, 公開日: 2003-02-04, 最終更新日: 2024-10-30)

主引用文献

Sevcik, J.,Urbanikova, L.,Leland, P.A.,Raines, R.T.
Links X-ray Structure of Two Crystalline Forms of a Streptomycete Ribonuclease with Cytotoxic Activity
J.Biol.Chem., 277:47325-47330, 2002

PubMed Abstract: Ribonuclease (RNase) Sa3 is secreted by the Gram-positive bacterium Streptomyces aureofaciens. The enzyme catalyzes the cleavage of RNA on the 3' side of guanosine residues. Here, x-ray diffraction analysis was used to determine the three-dimensional structure of two distinct crystalline forms of RNase Sa3 to a resolution of 2.0 and 1.7 A. These two structures are similar to each other as well as to that of a homolog, RNase Sa. All of the key active-site residues of RNase Sa (Asn(42), Glu(44), Glu(57), Arg(72), and His(88)) are located in the putative active site of RNase Sa3. Also herein, RNase Sa3 is shown to be toxic to human erythroleukemia cells in culture. Like onconase, which is an amphibian ribonuclease in Phase III clinical trials as a cancer chemotherapeutic, RNase Sa3 is not inhibited by the cytosolic ribonuclease inhibitor protein. Thus, a prokaryotic ribonuclease can be toxic to mammalian cells.

PubMed: 12228255
DOI: 10.1074/jbc.M208425200

実験手法

X-RAY DIFFRACTION (1.7 Å)