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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
11
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pubmed:dateCreated |
2001-10-30
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pubmed:databankReference |
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pubmed:abstractText |
A new group of error-prone DNA polymerases overcomes the blockage posed to normal DNA replication by damaged template bases, suggesting an active site with a loose, flexible pocket that accommodates aberrant DNA structures. We have determined a 2.8 A resolution crystal structure of the Sulfolobus solfataricus Dbh protein, a DNA translesion polymerase closely related to Escherichia coli DNA polymerase IV and human polymerase kappa. A high error rate is observed for the Dbh polymerase in a range of 10(-2)-10(-3) for all 12 base substitution mispairs. The crystal structure of Dbh reveals an overall architecture resembling other DNA polymerases but has unique features that are likely to contribute to error-prone synthesis, including -1 frameshifting mutations.
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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/Archaeal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Polymerase beta,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Directed DNA Polymerase,
http://linkedlifedata.com/resource/pubmed/chemical/Dbh protein, Sulfolobus solfataricus,
http://linkedlifedata.com/resource/pubmed/chemical/DinB protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/POLK protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Taq Polymerase
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
1072-8368
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
8
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
984-9
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11685247-Amino Acid Sequence,
pubmed-meshheading:11685247-Archaeal Proteins,
pubmed-meshheading:11685247-Bacterial Proteins,
pubmed-meshheading:11685247-Catalysis,
pubmed-meshheading:11685247-Conserved Sequence,
pubmed-meshheading:11685247-Crystallography, X-Ray,
pubmed-meshheading:11685247-DNA Polymerase beta,
pubmed-meshheading:11685247-DNA-Directed DNA Polymerase,
pubmed-meshheading:11685247-Escherichia coli Proteins,
pubmed-meshheading:11685247-Humans,
pubmed-meshheading:11685247-Kinetics,
pubmed-meshheading:11685247-Models, Molecular,
pubmed-meshheading:11685247-Molecular Sequence Data,
pubmed-meshheading:11685247-Mutagenesis,
pubmed-meshheading:11685247-Protein Structure, Tertiary,
pubmed-meshheading:11685247-Proteins,
pubmed-meshheading:11685247-Sequence Alignment,
pubmed-meshheading:11685247-Sequence Homology, Amino Acid,
pubmed-meshheading:11685247-Sulfolobus,
pubmed-meshheading:11685247-Taq Polymerase
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pubmed:year |
2001
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pubmed:articleTitle |
Crystal structure of a DinB family error-prone DNA polymerase from Sulfolobus solfataricus.
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pubmed:affiliation |
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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