Abstract
Bacteriophage T4 RNase H is a 5' to 3' exonuclease that removes RNA primers from the lagging strand of the DNA replication fork and is a member of the RAD2 family of eukaryotic and prokaryotic replication and repair nucleases. The crystal structure of the full-length native form of T4 RNase H has been solved at 2.06 angstroms resolution in the presence of Mg2+ but in the absence of nucleic acids. The most conserved residues are clustered together in a large cleft with two Mg2+ in the proposed active site. This structure suggests the way in which the widely separated conserved regions in the larger nucleotide excision repair proteins, such as human XPG, could assemble into a structure like that of the smaller replication nucleases.
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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Bacteriophage T4 / chemistry
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Bacteriophage T4 / enzymology*
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Binding Sites / physiology
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Crystallography
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DNA / metabolism
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DNA-Binding Proteins*
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DNA-Directed DNA Polymerase / chemistry
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Endodeoxyribonucleases / chemistry
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Exonucleases / chemistry*
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Fungal Proteins / chemistry*
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Image Processing, Computer-Assisted
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Magnesium / chemistry
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Metals / chemistry
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Metals / metabolism
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Molecular Sequence Data
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Protein Conformation
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Protein Structure, Secondary
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Protein Structure, Tertiary
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RNA / metabolism
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RNA-Directed DNA Polymerase / chemistry
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Ribonuclease H / chemistry*
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Saccharomyces cerevisiae Proteins*
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Sequence Homology, Amino Acid
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Taq Polymerase
Substances
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DNA-Binding Proteins
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Fungal Proteins
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Metals
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Saccharomyces cerevisiae Proteins
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RAD2 protein, S cerevisiae
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RNA
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DNA
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Taq Polymerase
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RNA-Directed DNA Polymerase
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DNA-Directed DNA Polymerase
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Endodeoxyribonucleases
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Exonucleases
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Ribonuclease H
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Magnesium