1tgo

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{{STRUCTURE_1tgo| PDB=1tgo | SCENE= }}
{{STRUCTURE_1tgo| PDB=1tgo | SCENE= }}
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'''THERMOSTABLE B TYPE DNA POLYMERASE FROM THERMOCOCCUS GORGONARIUS'''
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===THERMOSTABLE B TYPE DNA POLYMERASE FROM THERMOCOCCUS GORGONARIUS===
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==Overview==
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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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{{ABSTRACT_PUBMED_10097083}}
==About this Structure==
==About this Structure==
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[[Category: Dna polymerase]]
[[Category: Dna polymerase]]
[[Category: Replication]]
[[Category: Replication]]
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Revision as of 01:45, 28 July 2008

Template:STRUCTURE 1tgo

THERMOSTABLE B TYPE DNA POLYMERASE FROM THERMOCOCCUS GORGONARIUS

Template:ABSTRACT PUBMED 10097083

About this Structure

1TGO is a Single protein structure of sequence from Thermococcus gorgonarius. Full crystallographic information is available from OCA.

Reference

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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