1giu

A TRICHOSANTHIN(TCS) MUTANT(E85R) COMPLEX STRUCTURE WITH ADENINE

spinqualitylabelsall models 1giu, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1giu is a 1 chain structure with sequence from Chinese cucumber. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ADE Related: 1gis Activity: rRNA N-glycosylase, with EC number 3.2.2.22 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [RIPT_TRIKI] Inactivates eukaryotic 60S ribosomal subunits. 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 Trichosanthin (TCS) is a type I ribosome-inactivating protein (RIP) which possesses rRNA N-glycosidase activity. In recent years, its immunomodulatory, anti-tumor and anti-HIV properties have been revealed. Here we report the crystal structures of several E85 mutant TCS complexes with adenosine-5'-monophosphate (AMP) and adenine. In E85Q TCS/AMP and E85A TCS/AMP, near the active site of the molecule and parallel to the aromatic ring of Tyr70, an AMP molecule is bound to the mutant without being hydrolyzed. In the E85R TCS/adenine complex, the hydrolyzed product adenine is located in the active pocket where it occupies a position similar to that in the TCS/NADPH complex. Significantly, AMP is bound in a position different to that of adenine. In comparison with these structures, we suggest that there are at least two subsites in the active site of TCS, one for initial substrate recognition as revealed by the AMP site and another for catalysis as represented by the NADPH site. Based on these complex structures, the function of residue 85 and the mechanism of catalysis are proposed. Substrate binding and catalysis in trichosanthin occur in different sites as revealed by the complex structures of several E85 mutants.,Guo Q, Zhou W, Too HM, Li J, Liu Y, Bartlam M, Dong Y, Wong KB, Shaw PC, Rao Z Protein Eng. 2003 Jun;16(6):391-6. PMID:12874371 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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