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Crystal structure of a group I ribozyme domain: principles of RNA packing

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Crystal structure of a group I ribozyme domain: principles of RNA packing (English)

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8

J A Doudna

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author name string

J H Cate

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1

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A R Gooding

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2

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E Podell

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3

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K Zhou

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4

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B L Golden

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5

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C E Kundrot

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6

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T R Cech

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7

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language of work or name

English

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publication date

20 September 1996

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published in

Science

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273

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5282

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page(s)

1678-85

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cites work

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Model for an RNA tertiary interaction from the structure of an intermolecular complex between a GAAA tetraloop and an RNA helix.

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RNA - ligand interactions:(I) magnesium binding sites in yeast tRNAPhe

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RNA tertiary structure mediation by adenosine platforms

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Three-Dimensional Structure of Yeast Phenylalanine Transfer RNA: Folding of the Polynucleotide Chain

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Visualization of a tertiary structural domain of the Tetrahymena group I intron by electron microscopy

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Architecture of ribosomal RNA: constraints on the sequence of "tetra-loops"

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1H NMR studies of the high-affinity Rev binding site of the Rev responsive element of HIV-1 mRNA: base pairing in the core binding element

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Ribozymes: A Distinct Class of Metalloenzymes

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HIV-1 Rev regulation involves recognition of non-Watson-Crick base pairs in viral RNA.

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Metal ion requirements for sequence-specific endoribonuclease activity of the Tetrahymena ribozyme

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A tyrosyl-tRNA synthetase can function similarly to an RNA structure in the Tetrahymena ribozyme

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Metal coordination sites that contribute to structure and catalysis in the group I intron from Tetrahymena

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Iron(II)-ethylenediaminetetraacetic acid catalyzed cleavage of RNA and DNA oligonucleotides: similar reactivity toward single- and double-stranded forms

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RNA structure at high resolution

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Structural Features that Give Rise to the Unusual Stability of RNA Hairpins Containing GNRA Loops

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Movement of the Guide Sequence During RNA Catalysis by a Group I Ribozyme

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Evidence of natural selection to maintain a functional domain outside of the 'core' in a large subclass of group I introns

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RNA substrate binding site in the catalytic core of the Tetrahymena ribozyme

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Crystallization of ribozymes and small RNA motifs by a sparse matrix approach

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Representation of the secondary and tertiary structure of group I introns

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The origin of the genetic code

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Visualizing the higher order folding of a catalytic RNA molecule

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Structural conventions for group I introns

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Kinetic intermediates in RNA folding

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Metal ion requirements and other aspects of the reaction catalyzed by M1 RNA, the RNA subunit of ribonuclease P from Escherichia coli.

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Exocyclic amine of the conserved G.U pair at the cleavage site of the Tetrahymena ribozyme contributes to 5'-splice site selection and transition state stabilization

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An independently folding domain of RNA tertiary structure within the Tetrahymena ribozyme

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Multiple magnesium ions in the ribonuclease P reaction mechanism

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Metal ion catalysis in the Tetrahymena ribozyme reaction

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A crystallographic study of metal-binding to yeast phenylalanine transfer RNA

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Catalytic activity is retained in the Tetrahymena group I intron despite removal of the large extension of element P5.

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Improved methods for building protein models in electron density maps and the location of errors in these models

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Modelling of the three-dimensional architecture of group I catalytic introns based on comparative sequence analysis

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Frequent use of the same tertiary motif by self-folding RNAs

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Phylogenetic and genetic evidence for base-triples in the catalytic domain of group I introns

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Reconstitution of a group I intron self-splicing reaction with an activator RNA.

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Coaxially stacked RNA helices in the catalytic center of the Tetrahymena ribozyme

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Defining the inside and outside of a catalytic RNA molecule

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Structure of yeast phenylalanine tRNA at 3 Å resolution

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Tertiary Structure Around the Guanosine-Binding Site of the Tetrahymena Ribozyme

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The guanosine binding site of the Tetrahymena ribozyme

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Self-splicing of group I introns

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(Q27733326)

Crystal structure of a group I ribozyme domain: principles of RNA packing

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