Structural and functional insights provided by crystal structures of DNA polymerases and their substrate complexes.
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.
Brautigam
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Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8114, USA.
Steitz
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TA
D000595:Amino Acid Sequence; D003460:Crystallization; D018360:Crystallography, X-Ray; D004247:DNA / Q000737:chemistry / Q000378:metabolism*; D004259:DNA-Directed DNA Polymerase / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D011487:Protein Conformation; D016415:Sequence Alignment; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
D004247:DNA; D004259:DNA-Directed DNA Polymerase