Journal
FEBS LETTERS
Volume 470, Issue 3, Pages 239-243Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/S0014-5793(00)01325-9
Keywords
ribosome inactivating protein; toxin; N-glycosidase; molecular recognition; Saponaria officinalis
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The 2.0 Angstrom resolution crystal structure of the ribosome inactivating protein saporin (isoform 6) from seeds of Saponaria officinalis is presented. The fold typical of other plant toxins is conserved, despite some differences in the loop regions. The loop between strands beta 7 and beta 8 in the C-terminal region which spans over the active site cleft appears shorter in saporin, suggesting an easier access to the substrate. Furthermore,ve investigated the molecular interaction between saporin and the yeast ribosome by differential chemical modifications. A contact surface inside the C-terminal region of saporin has been identified. Structural comparison between saporin and other ribosome inactivating proteins reveals that this region is conserved and represents a peculiar motif involved in ribosome recognition. (C) 2000 Federation of European Biochemical Societies.
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