Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP.
Abstract:
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.
Polymerases:
Topics:
Structure and Structure/Function
Note:
First DNA polymerase crystal structure. (PDB file 1DPI)
Status:
| new | topics/pols set | partial results | complete | validated |
Results:
| Polymerase | Reference | Property | Result | Context |
|---|---|---|---|---|
| Klenow fragment | Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP. | Cloned or native | Cloned in E. coli | |
| Klenow fragment | Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP. | Tagged | No | |
| Klenow fragment | Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP. | Full length or truncated | Full length | |
| Klenow fragment | Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP. | Other Important Residues | dNMP-Zn interacts with D355, E357, T358, L361, D424, F473, Y497, D501 |