3hiv | pdb_00003hiv

Crystal structure of Saporin-L1 in complex with the trinucleotide inhibitor, a transition state analogue

spinqualitylabelsall models 3hiv, resolution 2.14Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3hiv is a 2 chain structure with sequence from Common soapwort. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: TXN Related: 3hio, 3hiq, 3his, 3hit, 3hiw Activity: rRNA N-glycosylase, with EC number 3.2.2.22 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 Ricin A-chain (RTA) and saporin-L1 (SAP) catalyze adenosine depurination of 28S rRNA to inhibit protein synthesis and cause cell death. We present the crystal structures of RTA and SAP in complex with transition state analogue inhibitors. These tight-binding inhibitors mimic the sarcin-ricin recognition loop of 28S rRNA and the dissociative ribocation transition state established for RTA catalysis. RTA and SAP share unique purine-binding geometry with quadruple pi-stacking interactions between adjacent adenine and guanine bases and 2 conserved tyrosines. An arginine at one end of the pi-stack provides cationic polarization and enhanced leaving group ability to the susceptible adenine. Common features of these ribosome-inactivating proteins include adenine leaving group activation, a remarkable lack of ribocation stabilization, and conserved glutamates as general bases for activation of the H(2)O nucleophile. Catalytic forces originate primarily from leaving group activation evident in both RTA and SAP in complex with transition state analogues. Transition state analogues in structures of ricin and saporin ribosome-inactivating proteins.,Ho MC, Sturm MB, Almo SC, Schramm VL Proc Natl Acad Sci U S A. 2009 Dec 1;106(48):20276-81. Epub 2009 Nov 17. PMID:19920175 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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