Structural and functional insights provided by crystal structures of DNA polymerases and their substrate complexes

被引：313

作者：

Brautigam, CA

Steitz, TA

机构：

[1] Yale Univ, Dept Mol Biophys & Biochem, New Haven, CT 06520 USA

[2] Yale Univ, Dept Chem, New Haven, CT 06520 USA

[3] Yale Univ, Howard Hughes Med Inst, New Haven, CT 06520 USA

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 1998年 / 8卷 / 01期

关键词：

D O I：

10.1016/S0959-440X(98)80010-9

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

New levels in the understanding of DNA replication have been achieved from recent crystal structure determinations of several DNA polymerases and their substrate complexes. The structure of an alpha family DNA polymerase from bacteriophage RB69 shows some similarities, but also considerable differences in structure and organization from the pol I family DNA polymerases. Also, the functions of three polymerase domains and their conserved residues have been clarified by studying structures of pol I family DNA polymerases complexed to their substrates. These structures also confirm that an identical two-metal ion catalytic mechanism proposed previously is used by both the nonhomologous pol I and pol beta family DNA polymerases.

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页码：54 / 63

页数：10

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