C. Savino et al., The crystal structure of saporin SO6 from Saponaria officinalis and its interaction with the ribosome, FEBS LETTER, 470(3), 2000, pp. 239-243
The 2.0 Angstrom resolution crystal structure of the ribosome inactivating
protein saporin (isoform 6) from seeds of Saponaria officinalis is presente
d. The fold typical of other plant toxins is conserved, despite some differ
ences in the loop regions. The loop between strands beta 7 and beta 8 in th
e C-terminal region which spans over the active site cleft appears shorter
in saporin, suggesting an easier access to the substrate. Furthermore,ve in
vestigated the molecular interaction between saporin and the yeast ribosome
by differential chemical modifications. A contact surface inside the C-ter
minal region of saporin has been identified. Structural comparison between
saporin and other ribosome inactivating proteins reveals that this region i
s conserved and represents a peculiar motif involved in ribosome recognitio
n. (C) 2000 Federation of European Biochemical Societies.