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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 |
1999-5-12
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pubmed:databankReference |
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pubmed:abstractText |
Most known archaeal DNA polymerases belong to the type B family, which also includes the DNA replication polymerases of eukaryotes, but maintain high fidelity at extreme conditions. We describe here the 2.5 A resolution crystal structure of a DNA polymerase from the Archaea Thermococcus gorgonarius and identify structural features of the fold and the active site that are likely responsible for its thermostable function. Comparison with the mesophilic B type DNA polymerase gp43 of the bacteriophage RB69 highlights thermophilic adaptations, which include the presence of two disulfide bonds and an enhanced electrostatic complementarity at the DNA-protein interface. In contrast to gp43, several loops in the exonuclease and thumb domains are more closely packed; this apparently blocks primer binding to the exonuclease active site. A physiological role of this "closed" conformation is unknown but may represent a polymerase mode, in contrast to an editing mode with an open exonuclease site. This archaeal B DNA polymerase structure provides a starting point for structure-based design of polymerases or ligands with applications in biotechnology and the development of antiviral or anticancer agents.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/10097083-1310946,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10097083-1323237,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10097083-1377403,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/10097083-9826686
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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 |
Mar
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
30
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pubmed:volume |
96
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3600-5
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:10097083-Amino Acid Sequence,
pubmed-meshheading:10097083-Binding Sites,
pubmed-meshheading:10097083-Cloning, Molecular,
pubmed-meshheading:10097083-Computer Graphics,
pubmed-meshheading:10097083-Conserved Sequence,
pubmed-meshheading:10097083-Crystallography, X-Ray,
pubmed-meshheading:10097083-DNA Polymerase I,
pubmed-meshheading:10097083-Enzyme Stability,
pubmed-meshheading:10097083-Hot Temperature,
pubmed-meshheading:10097083-Models, Molecular,
pubmed-meshheading:10097083-Molecular Sequence Data,
pubmed-meshheading:10097083-Protein Structure, Secondary,
pubmed-meshheading:10097083-Recombinant Proteins,
pubmed-meshheading:10097083-Sequence Alignment,
pubmed-meshheading:10097083-Sequence Homology, Amino Acid,
pubmed-meshheading:10097083-Thermococcus,
pubmed-meshheading:10097083-Thermodynamics
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pubmed:year |
1999
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pubmed:articleTitle |
Crystal structure of a thermostable type B DNA polymerase from Thermococcus gorgonarius.
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pubmed:affiliation |
Abteilung Strukturforschung, Max-Planck-Institut für Biochemie, D-82152 Martinsried, Germany. hopfner@scripps.edu
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pubmed:publicationType |
Journal Article,
Comparative Study
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