1DPI

STRUCTURE OF LARGE FRAGMENT OF ESCHERICHIA COLI DNA POLYMERASE I COMPLEXED WITH D/TMP

Summary for 1DPI

• Entry DOI: 10.2210/pdb1dpi/pdb
• Descriptor: DNA POLYMERASE I KLENOW FRAGMENT, ZINC ION (2 entities in total)
• Functional Keywords: nucleotidyltransferase
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 68227.10

Authors

Beese, L.,Ollis, D.,Steitz, T. (deposition date: 1987-08-11, release date: 1987-10-16, Last modification date: 2024-02-07)

Primary citation

Ollis, D.L.,Brick, P.,Hamlin, R.,Xuong, N.G.,Steitz, T.A.
Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP.
Nature, 313:762-766, 1985

PubMed 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.

PubMed: 3883192
DOI: 10.1038/313762a0

Experimental method

X-RAY DIFFRACTION (2.8 Å)