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