Abstract
The 3.3-Å resolution crystal structure of the large proteolytic fragment of Escherichia coli DNA polymerase I complexed with deoxythymidine monophosphate consists of two domains, the smaller of which binds zinc-deoxythymidine monophosphate. The most striking feature of the larger domain is a deep crevice of the appropriate size and shape for binding double-stranded B-DNA. A flexible subdomain may allow the enzyme to surround completely the DNA substrate, thereby allowing processive nucleotide polymerization without enzyme dissociation.
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Ollis, D., Brick, P., Hamlin, R. et al. Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP. Nature 313, 762–766 (1985). https://doi.org/10.1038/313762a0
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DOI: https://doi.org/10.1038/313762a0
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