The crystal structure of saporin SO6 from Saponaria officinalis and its interaction with the ribosome

FEBS Letters

Federici, Luca¹  Lendaro, Eugenio¹  Ippoliti, Rodolfo¹  Tsernoglou, Demetrius¹  Savino, Carmelinda¹ 

[1] Department of Biochemical Sciences and CNR Centre for Molecular Biology, University of Rome ‘La Sapienza’, Piazzale Aldo Moro 5, 00185 Rome, Italy

关键词: Ribosome inactivating protein;    Toxin;    N-Glycosidase;    Molecular recognition;    Saponaria officinalis;   

DOI  :  10.1016/S0014-5793(00)01325-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The 2.0 Å 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 β7 and β8 in the C-terminal region which spans over the active site cleft appears shorter in saporin, suggesting an easier access to the substrate. Furthermore we 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.

【 授权许可】

Unknown