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Structure of Escherichia coli exonuclease I suggests how processivity is achieved

Nature Structural Biology volume 7, pages 1125–1128 (2000)Cite this article

Abstract

Exonuclease I (ExoI) from Escherichia coli is a monomeric enzyme that processively degrades single stranded DNA in the 3′ to 5′ direction and has been implicated in DNA recombination and repair. Determination of the structure of ExoI to 2.4 Å resolution using X-ray crystallography verifies the expected correspondence between a region of ExoI and the exonuclease (or proofreading) domains of the DNA polymerases. The overall fold of ExoI also includes two other regions, one of which extends the exonuclease domain and another that can be described as an elaborated SH3 domain. These three regions combine to form a molecule that is shaped like the letter C, although it also contains a segment that effectively converts the C into an O-like shape. The structure of ExoI thus provides additional support for the idea that DNA metabolizing enzymes achieve processivity by completely enclosing the DNA.

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Figure 1: ExoI is a member of the DnaQ superfamily.
Figure 2: The structure of ExoI.
Figure 3: Comparison of ExoI with DNA polymerase.
Figure 4: Substrate binding.

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Acknowledgements

We thank L. Gay for providing the DH5α genome and for excellent technical assistance, R. Kovall for assistance and critical reading of the manuscript, I. Korndoerfer and M. Elsliger for help with computing aspects, P. Kuhn and A. Cohen for help with data collection at the SSRL and R. Kingston for critical reading of the manuscript. This work was supported in part by an NIH grant (to B.W.M.) and is based in part upon data collected at SSRL which is funded by the DOE and the NIH.

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  1. Howard Hughes Medical Institute and Department of Physics, Institute of Molecular Biology, 1229 University of Oregon, Eugene, 97403-1229, Oregon, USA

    Wendy A. Breyer & Brian W. Matthews

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Correspondence to Brian W. Matthews.

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Breyer, W., Matthews, B. Structure of Escherichia coli exonuclease I suggests how processivity is achieved. Nat Struct Mol Biol 7, 1125–1128 (2000). https://doi.org/10.1038/81978

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