1si7 | pdb_00001si7

Structure of E. coli tRNA psi 13 pseudouridine synthase TruD

spinqualitylabelsall models 1si7, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1si7 is a 1 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. Gene: TRUD ("Bacillus coli" Migula 1895) Activity: Pseudouridylate synthase, with EC number 4.2.1.70 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 TruD, a recently discovered novel pseudouridine synthase in Escherichia coli, is responsible for modifying uridine13 in tRNA(Glu) to pseudouridine. It has little sequence homology with the other 10 pseudouridine synthases in E. coli which themselves have been grouped into four related protein families. Crystal structure determination of TruD revealed a two domain structure consisting of a catalytic domain that differs in sequence but is structurally very similar to the catalytic domain of other pseudouridine synthases and a second large domain (149 amino acids, 43% of total) with a novel alpha/beta fold that up to now has not been found in any other protein. Crystal structure of TruD, a novel pseudouridine synthase with a new protein fold.,Kaya Y, Del Campo M, Ofengand J, Malhotra A J Biol Chem. 2004 Apr 30;279(18):18107-10. Epub 2004 Mar 3. PMID:14999002 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Guide-independent Pseudouridine synthase Pseudouridine synthase 3D structures

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