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

Chad A Brautigam; Thomas A. Steitz

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

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

Chad A Brautigam, Thomas A. Steitz

Research output: Contribution to journal › Article › peer-review

343 Scopus citations

Abstract

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 α 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 β family DNA polymerases.

Original language	English (US)
Pages (from-to)	54-63
Number of pages	10
Journal	Current Opinion in Structural Biology
Volume	8
Issue number	1
DOIs	https://doi.org/10.1016/S0959-440X(98)80010-9
State	Published - Feb 1998

ASJC Scopus subject areas

Structural Biology
Molecular Biology

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

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title = "Structural and functional insights provided by crystal structures of DNA polymerases and their substrate complexes",

abstract = "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 α 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 β family DNA polymerases.",

author = "Brautigam, {Chad A} and Steitz, {Thomas A.}",

note = "Funding Information: The authors wish to thank S Doublie and T Ellenberger for providing data and figures in advance of publication, J Wang for providing figures and molecular models, and J Jager and J Pata for access to molecular models. This work was funded in pan by the American Cancer Society grant #BE-52K to TAS.",

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AU - Steitz, Thomas A.

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AB - 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 α 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 β family DNA polymerases.

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

Abstract

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