期刊论文详细信息
FEBS Letters | |
Structural basis for the catalytic mechanism and substrate specificity of the ribonuclease α‐sarcin | |
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
【 预 览 】
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RO201912020303683ZK.pdf | 336KB | download |