3T0O

Crystal Structure Analysis of Human RNase T2

3T0O の概要

• エントリーDOI: 10.2210/pdb3t0o/pdb
• 分子名称: Ribonuclease T2, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• 機能のキーワード: rnaset2, alpha/beta fold, ribonuclease, rna cleavage, hydrolase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted: O00584
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 28451.15

構造登録者

Thorn, A.,Kraetzner, R.,Steinfeld, R.,Sheldrick, G. (登録日: 2011-07-20, 公開日: 2012-07-11, 最終更新日: 2024-11-20)

主引用文献

Thorn, A.,Steinfeld, R.,Ziegenbein, M.,Grapp, M.,Hsiao, H.H.,Urlaub, H.,Sheldrick, G.M.,Gartner, J.,Kratzner, R.
Structure and activity of the only human RNase T2.
Nucleic Acids Res., 40:8733-8742, 2012

PubMed Abstract: Mutations in the gene of human RNase T2 are associated with white matter disease of the human brain. Although brain abnormalities (bilateral temporal lobe cysts and multifocal white matter lesions) and clinical symptoms (psychomotor impairments, spasticity and epilepsy) are well characterized, the pathomechanism of RNase T2 deficiency remains unclear. RNase T2 is the only member of the Rh/T2/S family of acidic hydrolases in humans. In recent years, new functions such as tumor suppressing properties of RNase T2 have been reported that are independent of its catalytic activity. We determined the X-ray structure of human RNase T2 at 1.6 Å resolution. The α+β core fold shows high similarity to those of known T2 RNase structures from plants, while, in contrast, the external loop regions show distinct structural differences. The catalytic features of RNase T2 in presence of bivalent cations were analyzed and the structural consequences of known clinical mutations were investigated. Our data provide further insight into the function of human RNase T2 and may prove useful in understanding its mode of action independent of its enzymatic activity.

PubMed: 22735700
DOI: 10.1093/nar/gks614

実験手法

X-RAY DIFFRACTION (1.59 Å)