Crystal structure of the RluD pseudouridine synthase catalytic module, an enzyme that modifies 23S rRNA and is essential for normal cell growth of Escherichia coli.

No abstract is available for this paper.

• Publication year

  2004

• Venue

  Journal of Molecular Biology

• Publication date

  2004-01-02

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1016/J.JMB.2003.10.003PMID 14659742
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• RNA-modifying enzymes.

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• Multiple sequence alignment with the Clustal series of programs

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• Ribosomal RNA pseudouridines and pseudouridine synthases

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• ProDom: Automated Clustering of Homologous Domains

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• Identification and site of action of the remaining four putative pseudouridine synthases in Escherichia coli.

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• Pseudouridines and pseudouridine synthases of the ribosome.

  2001cited by this paper
• Crystal Structure of the Ribosome at 5.5 Å Resolution

  2001cited by this paper
• Genome sequence of enterohaemorrhagic Escherichia coli O157:H7

  2001cited by this paper
• A second function for pseudouridine synthases: A point mutant of RluD unable to form pseudouridines 1911, 1915, and 1917 in Escherichia coli 23S ribosomal RNA restores normal growth to an RluD-minus strain.

  2001cited by this paper
• Unique structural and stabilizing roles for the individual pseudouridine residues in the 1920 region of Escherichia coli 23S rRNA.

  2000cited by this paper
• The structural basis for tRNA recognition and pseudouridine formation by pseudouridine synthase I

  2000cited by this paper
• The Protein Data Bank

  2000cited by this paper
• Isolation and Properties of Escherichia coli 23S‐RNA Pseudouridine 1911, 1915, 1917 Synthase (RluD)

  2000cited by this paper
• Functional importance of motif I of pseudouridine synthases: mutagenesis of aligned lysine and proline residues.

  2000cited by this paper
• Reciprocal-space solvent flattening

  1999cited by this paper
• Critical Aspartic Acid Residues in Pseudouridine Synthases*

  1999cited by this paper
• Novel Predicted RNA-Binding Domains Associated with the Translation Machinery

  1999cited by this paper
• The mechanism of pseudouridine synthase I as deduced from its interaction with 5-fluorouracil-tRNA.

  1999cited by this paper
• Automated MAD and MIR structure solution

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• Automated protein model building combined with iterative structure refinement

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• Functional Effect of Deletion and Mutation of theEscherichia coli Ribosomal RNA and tRNA Pseudouridine Synthase RluA*

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• A conserved aspartate of tRNA pseudouridine synthase is essential for activity and a probable nucleophilic catalyst.

  1998cited by this paper
• A pseudouridine synthase required for the formation of two universally conserved pseudouridines in ribosomal RNA is essential for normal growth of Escherichia coli.

  1998cited by this paper
• Comparative studies of protein crystallization by vapour-diffusion and microbatch techniques.

  1998cited by this paper
• Identification of two Escherichia coli pseudouridine synthases that show multisite specificity for 23S RNA.

  1998cited by this paper
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• A Conserved Aspartate of tRNA Pseudouridine Synthase Is Essential for Activity and a Probable Nucleophilic Catalyst

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  1997cited by this paper
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  1996cited by this paper
• Pseudouridine synthases: four families of enzymes containing a putative uridine-binding motif also conserved in dUTPases and dCTP deaminases.

  1996cited by this paper
• RNA Chaperones and the RNA Folding Problem (*)

  1995cited by this paper
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  1995cited by this paper
• The single pseudouridine residue in Escherichia coli 16S RNA is located at position 516.

  1994cited by this paper
• PROCHECK: a program to check the stereochemical quality of protein structures

  1993cited by this paper
• Protein structure comparison by alignment of distance matrices.

  1993cited by this paper
• The gene for a tRNA modifying enzyme, m5U54-methyltransferase, is essential for viability in Escherichia coli.

  1992cited by this paper
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  1991cited by this paper
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  1991cited by this paper
• A program to produce both detailed and schematic plots of protein structures

  1991cited by this paper
• The numerous modified nucleotides in eukaryotic ribosomal RNA.

  1990cited by this paper
• Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): a vehicle for direct determination of three‐dimensional structure.

  1990cited by this paper
• Purification, structure, and properties of Escherichia coli tRNA pseudouridine synthase I.

  1988cited by this paper
• Electronic Reprint Biological Crystallography the Protein Data Bank Biological Crystallography the Protein Data Bank

  year unknowncited by this paper

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• Pseudouridines of tRNA Anticodon Stem-Loop Have Unexpected Role in Mutagenesis in Pseudomonas sp.

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• Post-transcriptional pseudouridylation in mRNA as well as in some major types of noncoding RNAs.

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• Loss of Pseudouridine Synthases in the RluA Family Causes Hypersensitive Nociception in Drosophila

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• The Role of Noncoding RNA Pseudouridylation in Nuclear Gene Expression Events

  2018cites this paper
• The role of S4-like RNA-binding and catalytic domains in the activity and specificity of bacterial pseudouridine synthases RluC and RluD in vitro

  2015cites this paper
• LOODUS- JA TEHNOLOOGIATEADUSKOND MOLEKULAAR- JA RAKUBIOLOOGIA INSTITUUT MOLEKULAARBIOLOOGIA ÕPPETOOL

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• Pseudouridines in spliceosomal snRNAs

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• Functional and structural impact of target uridine substitutions on the H/ACA ribonucleoprotein particle pseudouridine synthase.

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