Abstract
The structure of I-Crel provides the first view of a protein encoded by a gene within an intron. This endonuclease recognizes a long DNA site approximately 20 base pairs in length and facilitates the lateral transfer of that intron. The protein exhibits a DNA-binding surface consisting of four antiparallel beta-strands that form a 20 A wide groove which is over 70 A long. The architecture of this fold is different from that of the TATA binding protein, TBP, which also contains an antiparallel beta-saddle. The conserved LAGLIDADG motif, which is found in many mobile intron endonucleases, maturases and inteins, forms a novel helical interface and contributes essential residues to the active site.
Publication types
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Comparative Study
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Binding Sites
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Conserved Sequence
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Crystallography, X-Ray
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DNA / metabolism*
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DNA Restriction Enzymes*
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Deoxyribonuclease EcoRI / chemistry
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Deoxyribonuclease EcoRI / metabolism
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Deoxyribonucleases, Type II Site-Specific / chemistry*
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Deoxyribonucleases, Type II Site-Specific / genetics
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Deoxyribonucleases, Type II Site-Specific / metabolism*
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Dimerization
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Eukaryotic Cells / enzymology
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Introns*
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Models, Molecular
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Molecular Sequence Data
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Protein Conformation
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Protein Folding
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Substrate Specificity
Substances
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Recombinant Proteins
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DNA
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DNA Restriction Enzymes
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Deoxyribonuclease EcoRI
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endodeoxyribonuclease CreI
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Deoxyribonucleases, Type II Site-Specific