Abstract
A novel class of DNA-binding domains has been established from at least sixteen recently identified DNA-binding proteins. The three-dimensional structure of one of these domains, Mrf-2, has been solved using NMR methods. This structure is significantly different from known DNA-binding domain structures. The mechanism of DNA recognition by this motif has been suggested based on conserved residues, surface electrostatic potentials and chemical shift changes. This new DNA-binding motif shares structural homology with T4 RNase H, E. coli endonuclease III and Bacillus subtilis DNA polymerase I. The structural homology suggests a mechanism for substrate recognition by these enzymes.
Publication types
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Research Support, Non-U.S. Gov't
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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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Bacillus subtilis / enzymology
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Bacteriophage T4 / enzymology
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Conserved Sequence / genetics
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Crystallography, X-Ray
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DNA Polymerase I / chemistry*
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DNA Repair
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DNA Replication
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DNA-Binding Proteins / chemistry*
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Deoxyribonuclease (Pyrimidine Dimer)
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Endodeoxyribonucleases / chemistry*
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Models, Molecular
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Molecular Sequence Data
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Nuclear Magnetic Resonance, Biomolecular
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Protein Structure, Tertiary
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Recombinant Fusion Proteins
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Ribonuclease H / chemistry*
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Sequence Alignment
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Transcription Factors / chemistry*
Substances
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DNA-Binding Proteins
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Recombinant Fusion Proteins
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Transcription Factors
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DNA Polymerase I
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Endodeoxyribonucleases
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Deoxyribonuclease (Pyrimidine Dimer)
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Ribonuclease H