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

Nature (1985), Volume 313, Page 762

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 Ollis DL1985 Cloned or native Cloned in E. coli
Klenow fragment Ollis DL1985 Tagged No
Klenow fragment Ollis DL1985 Full length or truncated Full length
Klenow fragment Ollis DL1985 Other Important Residues dNMP-Zn interacts with D355, E357, T358, L361, D424, F473, Y497, D501

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