Structural highlights
Function
RIP6_SAPOF Ribosome-inactivating protein of type 1, inhibits protein synthesis in animal cells. Useful as immunotoxin for pharmacological applications.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
The crystal structure of saporin SO6 from Saponaria officinalis and its interaction with the ribosome.,Savino C, Federici L, Ippoliti R, Lendaro E, Tsernoglou D FEBS Lett. 2000 Mar 31;470(3):239-43. PMID:10745075[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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. 2000 Mar 31;470(3):239-43. PMID:10745075
