A coleopteran triosephosphate isomerase: X-ray structure and phylogenetic impact of insect sequences

Authors

  • D. Knobeloch,

    1. Institut für Biochemie, Charité– Universitätsmedizin Berlin, Berlin; and
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    • Both authors contributed equally to this paper.

    • §

      Present address: Biomedizinisches Forschungszentrum CVK, Charité– Universitätsmedizin Berlin, Berlin, Germany.

  • A. Schmidt,

    1. Institut für Biochemie, Charité– Universitätsmedizin Berlin, Berlin; and
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    • Both authors contributed equally to this paper.

  • P. Scheerer,

    1. Institut für Biochemie, Charité– Universitätsmedizin Berlin, Berlin; and
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    • Present address: Institut für Medizinische Physik und Biophysik (CC2), Charité– Universitätsmedizin Berlin, Berlin, Germany.

  • N. Krauss,

    1. Institut für Biochemie, Charité– Universitätsmedizin Berlin, Berlin; and
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    • **

      Present address: Queen Mary University of London, School of Biological and Chemical Sciences, London, UK.

  • H. Wessner,

    1. Institut für Biochemie, Charité– Universitätsmedizin Berlin, Berlin; and
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  • Ch. Scholz,

    1. Institut für Biochemie, Charité– Universitätsmedizin Berlin, Berlin; and
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  • G. Küttner,

    1. Institut für Biochemie, Charité– Universitätsmedizin Berlin, Berlin; and
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  • T. Von Rintelen,

    1. Museum für Naturkunde – Leibniz-Institut für Evolutions- und Biodiversitätsforschung an der Humboldt-Universität zu Berlin, Berlin, Germany
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  • A. Wessel,

    1. Museum für Naturkunde – Leibniz-Institut für Evolutions- und Biodiversitätsforschung an der Humboldt-Universität zu Berlin, Berlin, Germany
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  • W. Höhne

    Corresponding author
    1. Institut für Biochemie, Charité– Universitätsmedizin Berlin, Berlin; and
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Wolfgang Höhne, Institut für Biochemie, Charité– Universitätsmedizin Berlin, Monbijoustr. 2, D-10117 Berlin, Germany. Tel.: (+4930) 450 528153; fax: (+4930) 450 528909; e-mail: wolfgang.hoehne@charite.de

Abstract

A coleopteran triosephosphate isomerase (TIM) from Tenebrio molitor (yellow mealworm beetle) was recombinantly expressed in Escherichia coli and characterized with respect to thermal stability, kinetic parameters and oligomeric state. The enzyme was successfully crystallized and the structure determined by X-ray analysis to 2.0 Å resolution. This is the first example of an invertebrate TIM. We compare structural features with known structures of TIMs from microorganisms, plants and vertebrates, and discuss the utility of the Tenebrio TIM sequence, together with several newly sequenced insect TIMs, for molecular phylogenetic analysis.

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