1tgo: Difference between revisions
New page: left|200px<br /><applet load="1tgo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tgo, resolution 2.5Å" /> '''THERMOSTABLE B TYPE D... |
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[[Image:1tgo.jpg|left|200px]]<br /><applet load="1tgo" size=" | [[Image:1tgo.jpg|left|200px]]<br /><applet load="1tgo" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1tgo, resolution 2.5Å" /> | caption="1tgo, resolution 2.5Å" /> | ||
'''THERMOSTABLE B TYPE DNA POLYMERASE FROM THERMOCOCCUS GORGONARIUS'''<br /> | '''THERMOSTABLE B TYPE DNA POLYMERASE FROM THERMOCOCCUS GORGONARIUS'''<br /> | ||
==Overview== | ==Overview== | ||
Most known archaeal DNA polymerases belong to the type B family, which | 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. | ||
==About this Structure== | ==About this Structure== | ||
1TGO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermococcus_gorgonarius Thermococcus gorgonarius]. Active as [http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] Full crystallographic information is available from [http:// | 1TGO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermococcus_gorgonarius Thermococcus gorgonarius]. Active as [http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TGO OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Ankenbauer, W.]] | [[Category: Ankenbauer, W.]] | ||
[[Category: Eichinger, A.]] | [[Category: Eichinger, A.]] | ||
[[Category: Engh, R | [[Category: Engh, R A.]] | ||
[[Category: Hopfner, K | [[Category: Hopfner, K P.]] | ||
[[Category: Huber, R.]] | [[Category: Huber, R.]] | ||
[[Category: Laue, F.]] | [[Category: Laue, F.]] | ||
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[[Category: replication]] | [[Category: replication]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:13:20 2008'' | ||
Revision as of 16:13, 21 February 2008
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THERMOSTABLE B TYPE DNA POLYMERASE FROM THERMOCOCCUS GORGONARIUS
OverviewOverview
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.
About this StructureAbout this Structure
1TGO is a Single protein structure of sequence from Thermococcus gorgonarius. Active as DNA-directed DNA polymerase, with EC number 2.7.7.7 Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of a thermostable type B DNA polymerase from Thermococcus gorgonarius., Hopfner KP, Eichinger A, Engh RA, Laue F, Ankenbauer W, Huber R, Angerer B, Proc Natl Acad Sci U S A. 1999 Mar 30;96(7):3600-5. PMID:10097083
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