PMID:9808040

Citation	Yuan, YC, Whitson, RH, Liu, Q, Itakura, K and Chen, Y (1998) A novel DNA-binding motif shares structural homology to DNA replication and repair nucleases and polymerases. Nat. Struct. Biol. 5:959-64
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.
Links	PubMed Online version:10.1038/2934
Keywords	Amino Acid Sequence; Bacillus subtilis/enzymology; Bacteriophage T4/enzymology; Conserved Sequence/genetics; Crystallography, X-Ray; DNA Polymerase I/chemistry; DNA Repair; DNA Replication; DNA-Binding Proteins/chemistry; Deoxyribonuclease (Pyrimidine Dimer); Endodeoxyribonucleases/chemistry; Models, Molecular; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular; Protein Structure, Tertiary; Recombinant Fusion Proteins; Ribonuclease H/chemistry; Sequence Alignment; Transcription Factors/chemistry
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