1k8w | pdb_00001k8w

Crystal structure of the E. coli pseudouridine synthase TruB bound to a T stem-loop RNA

spinqualitylabelsall models 1k8w, resolution 1.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1k8w is a 2 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: SO4 NonStd Res: FHU Activity: Pseudouridylate synthase, with EC number 4.2.1.70 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [TRUB_ECOLI] Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs. 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 Pseudouridine (Psi) synthases catalyze the isomerization of specific uridines in cellular RNAs to pseudouridines and may function as RNA chaperones. TruB is responsible for the Psi residue present in the T loops of virtually all tRNAs. The close homolog Cbf5/dyskerin is the catalytic subunit of box H/ACA snoRNPs. These carry out the pseudouridylation of eukaryotic rRNA and snRNAs. The 1.85 A resolution structure of TruB bound to RNA reveals that this enzyme recognizes the preformed three-dimensional structure of the T loop, primarily through shape complementarity. It accesses its substrate uridyl residue by flipping out the nucleotide and disrupts the tertiary structure of tRNA. Structural comparisons with TruB demonstrate that all Psi synthases are descended from a common molecular ancestor. Cocrystal structure of a tRNA Psi55 pseudouridine synthase: nucleotide flipping by an RNA-modifying enzyme.,Hoang C, Ferre-D'Amare AR Cell. 2001 Dec 28;107(7):929-39. PMID:11779468 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also TRNA pseudouridine synthase

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