Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP.
The 3.3-A 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.
D001665:Binding Sites; D002412:Cations; D003460:Crystallization; D004247:DNA / Q000378:metabolism; D004256:DNA Polymerase I; D004268:DNA-Binding Proteins; D004926:Escherichia coli / Q000201:enzymology*; D008958:Models, Molecular; D010446:Peptide Fragments; D011487:Protein Conformation; D013942:Thymine Nucleotides / Q000378:metabolism; D014961:X-Ray Diffraction
D002412:Cations; D004268:DNA-Binding Proteins; D010446:Peptide Fragments; D013942:Thymine Nucleotides; D004247:DNA; D004256:DNA Polymerase I