1qi7

THE CRYSTAL STRUCTURE AT 2.0 A OF SAPORIN SO6, A RIBOSOME INACTIVATING PROTEIN FROM SAPONARIA OFFICINALIS

spinqualitylabelsall models 1qi7, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1qi7 is a 1 chain structure with sequence from Saponaria officinalis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: SO4 Activity: rRNA N-glycosylase, with EC number 3.2.2.22 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [RIP2_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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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