2b4v | pdb_00002b4v

Structural Basis for UTP Specificity of RNA Editing TUTases From Trypanosoma Brucei

spinqualitylabelsall models 2b4v, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2b4v is a 1 chain structure with sequence from Trypanosoma brucei. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Ligands: K, MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TUT2_TRYBB Terminal uridylyltransferase which, as part of the mitochondrial RNA editing core complex (RECC), is involved in the post-transcriptional editing of mitochondrial RNA, a process involving the addition and deletion of uridine (U) nucleotides in the pre-mRNA (PubMed:12820966, PubMed:19465686, PubMed:20362585). Specifically, catalyzes the addition of one U to single-stranded RNA with a preference for a 3'-terminal A or G and adds the number of Us specified by a guide RNA (gRNA) to precleaved double-stranded RNA editing substrates (PubMed:12820966, PubMed:19465686, PubMed:20362585, PubMed:16281058). Essential for the survival of the bloodstream form (PubMed:16281058). 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 Trypanosomatids are pathogenic protozoa that undergo a unique form of post-transcriptional RNA editing that inserts or deletes uridine nucleotides in many mitochondrial pre-mRNAs. Editing is catalyzed by a large multiprotein complex, the editosome. A key editosome enzyme, RNA editing terminal uridylyl transferase 2 (TUTase 2; RET2) catalyzes the uridylate addition reaction. Here, we report the 1.8 A crystal structure of the Trypanosoma brucei RET2 apoenzyme and its complexes with uridine nucleotides. This structure reveals that the specificity of the TUTase for UTP is determined by a crucial water molecule that is exquisitely positioned by the conserved carboxylates D421 and E424 to sense a hydrogen atom on the N3 position of the uridine base. The three-domain structure also unveils a unique domain arrangement not seen before in the nucleotidyltansferase superfamily, with a large domain insertion between the catalytic aspartates. This insertion is present in all trypanosomatid TUTases. We also show that TbRET2 is essential for survival of the bloodstream form of the parasite and therefore is a potential target for drug therapy. Structural basis for UTP specificity of RNA editing TUTases from Trypanosoma brucei.,Deng J, Ernst NL, Turley S, Stuart KD, Hol WG EMBO J. 2005 Dec 7;24(23):4007-17. Epub 2005 Nov 10. PMID:16281058 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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