Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP

Abstract
The 3.3-.ANG. resolution crystal structure of the large proteolytic fragment of E. coli DNA polymerase I complexed with deoxythymidine monophosphate consists of 2 domains, the smaller of which binds Zn-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, allowing processive nucleotide polymerization without enzyme dissociation.