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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
7
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pubmed:dateCreated |
1996-8-14
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pubmed:databankReference |
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pubmed:abstractText |
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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Directed DNA Polymerase,
http://linkedlifedata.com/resource/pubmed/chemical/Endodeoxyribonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/Exonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Magnesium,
http://linkedlifedata.com/resource/pubmed/chemical/Metals,
http://linkedlifedata.com/resource/pubmed/chemical/RAD2 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/RNA,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Directed DNA Polymerase,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonuclease H,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Taq Polymerase
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0092-8674
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
28
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pubmed:volume |
85
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1101-12
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:8674116-Bacteriophage T4,
pubmed-meshheading:8674116-Binding Sites,
pubmed-meshheading:8674116-Crystallography,
pubmed-meshheading:8674116-DNA,
pubmed-meshheading:8674116-DNA-Binding Proteins,
pubmed-meshheading:8674116-DNA-Directed DNA Polymerase,
pubmed-meshheading:8674116-Endodeoxyribonucleases,
pubmed-meshheading:8674116-Exonucleases,
pubmed-meshheading:8674116-Fungal Proteins,
pubmed-meshheading:8674116-Image Processing, Computer-Assisted,
pubmed-meshheading:8674116-Magnesium,
pubmed-meshheading:8674116-Metals,
pubmed-meshheading:8674116-Molecular Sequence Data,
pubmed-meshheading:8674116-Protein Conformation,
pubmed-meshheading:8674116-Protein Structure, Secondary,
pubmed-meshheading:8674116-Protein Structure, Tertiary,
pubmed-meshheading:8674116-RNA,
pubmed-meshheading:8674116-RNA-Directed DNA Polymerase,
pubmed-meshheading:8674116-Ribonuclease H,
pubmed-meshheading:8674116-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:8674116-Sequence Homology, Amino Acid,
pubmed-meshheading:8674116-Taq Polymerase
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pubmed:year |
1996
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pubmed:articleTitle |
Structure of bacteriophage T4 RNase H, a 5' to 3' RNA-DNA and DNA-DNA exonuclease with sequence similarity to the RAD2 family of eukaryotic proteins.
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pubmed:affiliation |
Laboratory of Structural Biology Research, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland 20892-2755, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.
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