Nature. 1985 Feb 28-Mar 6;313(6005):762-6.

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

Ollis DL, Brick P, Hamlin R, Xuong NG, Steitz TA.

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.

PMID:: 3883192; [PubMed - indexed for MEDLINE]

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Structures reported by this article

Dna Polymerase I Klenow Fragment (E.C.2.7.7.7) MutantDNA Complex

PDB: 1KLN

Source: Escherichia coli, synthetic construct

Method: X-Ray Diffraction

Resolution: 3.2 Å

See all 3 structures...

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

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