1sb7 | pdb_00001sb7

Crystal structure of the E.coli pseudouridine synthase TruD

spinqualitylabelsall models 1sb7, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1sb7 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: GOL, PO4 NonStd Res: MSE Gene: TRUD, B2745 ("Bacillus coli" Migula 1895) Activity: Pseudouridylate synthase, with EC number 4.2.1.70 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [TRUD_ECOLI] Responsible for synthesis of pseudouridine from uracil-13 in 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 The pseudouridine (Psi) synthases Pus7p and TruD define a family of RNA-modifying enzymes with no sequence similarity to previously characterized Psi synthases. The 2.2 A resolution structure of Escherichia coli TruD reveals a U-shaped molecule with a catalytic domain that superimposes closely on that of other Psi synthases. A domain that appears to be unique to TruD/Pus7p family enzymes hinges over the catalytic domain, possibly serving to clasp the substrate RNAs. The active site comprises residues that are conserved in other Psi synthases, although at least one comes from a structurally distinct part of the protein. Remarkably, the connectivity of the structural elements of the TruD catalytic domain is a circular permutation of that of its paralogs. Because the sequence of the permuted segment, a beta-strand that bisects the catalytic domain, is conserved among orthologs from bacteria, archaea and eukarya, the permutation likely happened early in evolution. Crystal structure of the highly divergent pseudouridine synthase TruD reveals a circular permutation of a conserved fold.,Hoang C, Ferre-D'Amare AR RNA. 2004 Jul;10(7):1026-33. PMID:15208439 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also TRNA pseudouridine synthase

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