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2.1 Å structure of Serratia endonuclease suggests a mechanism for binding to double-stranded DNA

Nature Structural Biology volume 1, pages 461–468 (1994)Cite this article

Abstract

The crystal structure of Serratia endonuclease has been solved to 2.1 Å by multiple isomorphous replacement. This magnesium-dependent enzyme is equally active against single- and double-stranded DNA, as well as RNA, without any apparent base preference. The Serratia endonuclease fold is distinct from that of other nucleases that have been solved by X-ray diffraction. The refined structure consists of a central layer containing six antiparallel β-strands which is flanked on one side by a helical domain and on the opposite side by one dominant helix and a very long coiled loop. Electrostatic calculations reveal a strongly polarized molecular surface and suggest that a cleft between this long helix and loop, near His 89, may contain the active site of the enzyme.

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Authors and Affiliations

  1. Department of Biochemical and Biophysical Sciences, University of Houston, Houston, Texas, 77204-5934, U.S.A.

    Mitchell D. Miller, Jack Tanner, Mary Alpaugh, Michael J. Benedik & Kurt L. Krause

  2. Department of Medicine, Baylor College of Medicine, Houston, Texas, 77030, USA

    Kurt L. Krause

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  1. Mitchell D. Miller
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  4. Michael J. Benedik
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  5. Kurt L. Krause
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Miller, M., Tanner, J., Alpaugh, M. et al. 2.1 Å structure of Serratia endonuclease suggests a mechanism for binding to double-stranded DNA. Nat Struct Mol Biol 1, 461–468 (1994). https://doi.org/10.1038/nsb0794-461

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