期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 16, 期 9, 页码 979-U107出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.1663
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资金
- US National Institutes of Health [CA138546]
- NATIONAL CANCER INSTITUTE [R01CA138546] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF BIOMEDICAL IMAGING AND BIOENGINEERING [P30EB009998] Funding Source: NIH RePORTER
DNA polymerase. (Pol delta) is a high-fidelity polymerase that has a central role in replication from yeast to humans. We present the crystal structure of the catalytic subunit of yeast Pol delta in ternary complex with a template primer and an incoming nucleotide. The structure, determined at 2.0-angstrom resolution, catches the enzyme in the act of replication, revealing how the polymerase and exonuclease domains are juxtaposed relative to each other and how a correct nucleotide is selected and incorporated. The structure also reveals the 'sensing' interactions near the primer terminus, which signal a switch from the polymerizing to the editing mode. Taken together, the structure provides a chemical basis for the bulk of DNA synthesis in eukaryotic cells and a framework for understanding the effects of cancer-causing mutations in Pol delta.
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