1QI7
THE CRYSTAL STRUCTURE AT 2.0 A OF SAPORIN SO6, A RIBOSOME INACTIVATING PROTEIN FROM SAPONARIA OFFICINALIS
Summary for 1QI7
| Entry DOI | 10.2210/pdb1qi7/pdb |
| Descriptor | PROTEIN (N-GLYCOSIDASE), SULFATE ION (3 entities in total) |
| Functional Keywords | ribosome inactivating protein, n-glycosidase, hydrolase |
| Biological source | Saponaria officinalis (common soapwort) |
| Total number of polymer chains | 1 |
| Total formula weight | 28720.80 |
| Authors | Savino, C.,Federici, L.,Ippoliti, R.,Lendaro, E.,Tsernoglou, D. (deposition date: 1999-06-08, release date: 2000-06-05, Last modification date: 2023-08-16) |
| Primary citation | Savino, C.,Federici, L.,Ippoliti, R.,Lendaro, E.,Tsernoglou, D. The crystal structure of saporin SO6 from Saponaria officinalis and its interaction with the ribosome. FEBS Lett., 470:239-243, 2000 Cited by PubMed Abstract: The 2.0 A 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 beta7 and beta8 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. PubMed: 10745075DOI: 10.1016/S0014-5793(00)01325-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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