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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4975
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pubmed:dateCreated |
1990-10-26
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pubmed:abstractText |
Ribonuclease H digests the RNA strand of duplex RNA.DNA hybrids into oligonucleotides. This activity is indispensable for retroviral infection and is involved in bacterial replication. The ribonuclease H from Escherichia coli is homologous with the retroviral proteins. The crystal structure of the E. coli enzyme reveals a distinctive alpha-beta tertiary fold. Analysis of the molecular model implicates a carboxyl triad in the catalytic mechanism and suggests a likely mode for the binding of RNA.DNA substrates. The structure was determined by the method of multiwavelength anomalous diffraction (MAD) with the use of synchrotron data from a crystal of the recombinant selenomethionyl protein.
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pubmed:grant |
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0036-8075
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
21
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pubmed:volume |
249
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1398-405
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:2169648-Amino Acid Sequence,
pubmed-meshheading:2169648-Binding Sites,
pubmed-meshheading:2169648-Computer Graphics,
pubmed-meshheading:2169648-Endoribonucleases,
pubmed-meshheading:2169648-Escherichia coli,
pubmed-meshheading:2169648-Models, Molecular,
pubmed-meshheading:2169648-Molecular Sequence Data,
pubmed-meshheading:2169648-Protein Conformation,
pubmed-meshheading:2169648-Recombinant Proteins,
pubmed-meshheading:2169648-Ribonuclease H,
pubmed-meshheading:2169648-Selenium,
pubmed-meshheading:2169648-Selenomethionine,
pubmed-meshheading:2169648-Sequence Homology, Nucleic Acid,
pubmed-meshheading:2169648-X-Ray Diffraction
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pubmed:year |
1990
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pubmed:articleTitle |
Structure of ribonuclease H phased at 2 A resolution by MAD analysis of the selenomethionyl protein.
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pubmed:affiliation |
Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.
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