Structural basis for the catalytic mechanism and substrate specificity of the ribonuclease α‐sarcin

FEBS Letters

Santoro, Jorge¹  Martínez del Pozo, Alvaro²  Lacadena, Javier²  Bruix, Marta¹  Campos-Olivas, Ramón¹  Gavilanes, JoséG.²  Rico, Manuel¹ 

[1] Instituto de Estructura de la Materia, Consejo Superior de Investigaciones Científicas, Serrano 119, 28006 Madrid, Spain;Departamento de Bioquímica y Biología Molecular I, Facultad de Química, Universidad Complutense, 28040 Madrid, Spain

关键词: Ribosome inactivating protein;    α-Sarcin;    Three-dimensional structure;    NMR;    Ribonuclease specificity;   

DOI  :  10.1016/S0014-5793(96)01320-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

α-Sarcin is a ribosome-inactivating protein which selectively cleaves a single phosphodiester bond in a universally conserved sequence of the major rRNA. The solution structure of α-sarcin has been determined on the basis of 1898 distance and angular experimental constraints from NMR spectroscopy. It reveals a catalytic mechanism analogous to that of the T₁ family of ribonucleases while its exquisite specificity resides in the contacts provided by its distinctive loops.

【 授权许可】

Unknown