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Structure and function of glutamyl-tRNA reductase, the first enzyme of tetrapyrrole biosynthesis in plants and prokaryotes

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Abstract

Glutamyl-tRNA reductase (GluTR) catalyzes the first step of tetrapyrrole biosynthesis in plants, archaea and most bacteria. The catalytic mechanism of the enzyme was elucidated both by biochemical data and the determination of the high-resolution crystal structure of the enzyme from the archaeon Methanopyrus kandleri in complex with a competitive inhibitor. The dimeric enzyme has an unusual V-shaped architecture where each monomer consists of three domains linked by a long `spinal' α-helix. The central catalytic domain specifically recognizes the glutamate moiety of the substrate. It bears a conserved cysteine poised to nucleophilically attack the activated aminoacyl bond of glutamyl-tRNA. Subsequently, the thioester intermediate is reduced to the product glutamate-1-semialdehyde via hydride transfer from NADPH supplied by the second domain. A structure-based sequence alignment indicates that catalytically essential amino acids are conserved throughout all GluTRs. Thus the catalytic mechanism derived for M. kandleri is common to all including plant GluTRs. Mutations described to influence the catalytic efficiency of the barley enzyme can therefore be explained.

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Authors and Affiliations

  1. Department of Structural Biology, German Research Center for Biotechnology, Mascheroder Weg 1, 38104, Braunschweig, Germany

    Wolf-Dieter Schubert & Dirk W. Heinz

  2. Institute of Microbiology, Technical University Braunschweig, Spielmannstrasse 7, 38106, Braunschweig, Germany

    Jürgen Moser, Stefan Schauer & Dieter Jahn

Authors
  1. Wolf-Dieter Schubert
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  2. Jürgen Moser
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  3. Stefan Schauer
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  4. Dirk W. Heinz
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  5. Dieter Jahn
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Correspondence to Dieter Jahn.

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Schubert, WD., Moser, J., Schauer, S. et al. Structure and function of glutamyl-tRNA reductase, the first enzyme of tetrapyrrole biosynthesis in plants and prokaryotes. Photosynthesis Research 74, 205–215 (2002). https://doi.org/10.1023/A:1020963711861

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