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Flexible loops and helical arches

Nature Structural Biology volume 5, pages 668–670 (1998)Cite this article

Abstract

The crystal structure of an archaeal 5' flap endonuclease suggests a common mode of action in this divergent group of essential replicative enzymes.

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Figure 1: The flap endonucleases (5' nucleases) possess both exo- and endo-nucleolytic activity. Nicked substrates (top) can become strand displaced producing bifurcated, or flap, structures (middle).
Figure 2: Representations11, 12 of the folds of a, MjFEN-11, b, the exonuclease domain of Taq polymerase6, c, T4 RNAase H8 and d, T5 exonuclease7.
Figure 3: Superposed divalent metal binding sites in MjFEN (gray), RNase H (yellow), T5 exonuclease (green) and Taq polymerase (red).

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Authors and Affiliations

  1. the Division of Molecular & Genetic Medicine, University of Sheffield, Krebs Institute, Sheffield , S10 2JF, UK

    Jon R. Sayers

  2. the Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, S10 2JF, UK

    Peter J. Artymiuk

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  1. Jon R. Sayers
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  2. Peter J. Artymiuk
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Correspondence to Jon R. Sayers.

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Sayers, J., Artymiuk, P. Flexible loops and helical arches. Nat Struct Mol Biol 5, 668–670 (1998). https://doi.org/10.1038/1358

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