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Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/54396
Title: Structural basis for the catalytic mechanism and substrate specificity of the ribonuclease α-sarcin
Authors: Campos Olivas, Ramón; Bruix, M.; Santoro, Jorge; Martínez del Pozo, Alvaro; Lacadena, Javier; Gavilanes, José G.; Rico, Manuel
Issue Date: 1996
Publisher: Elsevier
Citation: FEBS Letters 399(1-2): 163- 165 (1996)
Abstract: -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.
URI: http://hdl.handle.net/10261/54396
DOI: 10.1016/S0014-5793(96)01320-8
Identifiers: doi: 10.1016/S0014-5793(96)01320-8
issn: 0014-5793
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