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Titolo:
Crystal structure of a thermostable type B DNA polymerase from Thermococcus gorgonarius
Autore:
Hopfner, KP; Eichinger, A; Engh, RA; Laue, F; Ankenbauer, W; Huber, R; Angerer, B;
Indirizzi:
Max Planck Inst Biochem, Abt Strukturforsch, D-82152 Martinsried, Germany Max Planck Inst Biochem Martinsried Germany D-82152 Martinsried, Germany Roche Diagnost, D-82372 Penzberg, Germany Roche Diagnost Penzberg Germany D-82372 gnost, D-82372 Penzberg, Germany
Titolo Testata:
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
fascicolo: 7, volume: 96, anno: 1999,
pagine: 3600 - 3605
SICI:
0027-8424(19990330)96:7<3600:CSOATT>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
REPLICATION FORK; ANGSTROM RESOLUTION; LARGE FRAGMENT; STRANDED-DNA; COMPLEX; BACTERIOPHAGE-T4; BETA; ARCHAEON; PRIMER; ALPHA;
Keywords:
x-ray structure; disulfide bonds; replication; Archaea; exonuclease;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
48
Recensione:
Indirizzi per estratti:
Indirizzo: Hopfner, KP Maxinsried,Inst Biochem, Abt Strukturforsch, Klopferspitz 18A,D-82152 Mart Max Planck Inst Biochem Klopferspitz 18A Martinsried GermanyD-82152
Citazione:
K.P. Hopfner et al., "Crystal structure of a thermostable type B DNA polymerase from Thermococcus gorgonarius", P NAS US, 96(7), 1999, pp. 3600-3605

Abstract

Most known archaeal DNA polymerases belong to the type B family, which also includes the DNA replication polymerases of eukaryotes, but maintain highfidelity at extreme conditions. We describe here the 2.5 Angstrom 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 domainsare 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 modewith an open exonuclease site. This archaeal 13 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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Documento generato il 22/09/20 alle ore 20:48:30