title: Structural basis for the catalytic mechanism and substrate specificity of the ribonuclease alpha-sarcin.
abstract: alpha-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 a-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.
authors.affiliation: Instituto de Estructura de la Materia, Consejo Superior de Investigaciones Científicas, Madrid, Spain.
authors.forename: R
authors.initials: R
authors.lastname: Campos-Olivas
authors.forename: M
authors.initials: M
authors.lastname: Bruix
authors.forename: J
authors.initials: J
authors.lastname: Santoro
authors.forename: A
authors.initials: A
authors.lastname: Martínez del Pozo
authors.forename: J
authors.initials: J
authors.lastname: Lacadena
authors.forename: J G
authors.initials: JG
authors.lastname: Gavilanes
authors.forename: M
authors.initials: M
authors.lastname: Rico
mesh_terms: D001665:Binding Sites; D002384:Catalysis; D004722:Endoribonucleases; D005656:Fungal Proteins / Q000737:chemistry / Q000378:metabolism*; D011487:Protein Conformation; D013379:Substrate Specificity
chemical_list: D005656:Fungal Proteins; C014801:alpha-sarcin; D004722:Endoribonucleases