The crystal structure of Escherichia coli spermidine synthase SpeE reveals a unique substrate-binding pocket |
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| Authors: | Xingding Zhou Teck Khiang Chua Karolina L Tkaczuk Janusz M Bujnicki J Sivaraman |
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| Institution: | 1. Department of Biological Sciences, 14 Science Drive 4, National University of Singapore, Singapore 117543, Republic of Singapore;2. Laboratory of Bioinformatics and Protein Engineering, International Institute of Molecular and Cell Biology in Warsaw, ul. Ks. Trojdena 4, 02-109 Warsaw, Poland;3. Institute of Technical Biochemistry, Technical University of Lodz, B. Stefanowskiego 4/10, 90-924 Lodz, Poland;4. Bioinformatics Laboratory, Institute of Molecular Biology and Biotechnology, Adam Mickiewicz University, Umultowska 89, 61-614 Poznan, Poland |
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| Abstract: | Polyamines are essential in all branches of life. Biosynthesis of spermidine, one of the most ubiquitous polyamines, is catalyzed by spermidine synthase (SpeE). Although the function of this enzyme from Escherichia coli has been thoroughly characterised, its structural details remain unknown. Here, we report the crystal structure of E. coli SpeE and study its interaction with the ligands by isothermal titration calorimetry and computational modelling. SpeE consists of two domains – a small N-terminal β-strand domain, and a C-terminal catalytic domain that adopts a canonical methyltransferase (MTase) Rossmann fold. The protein forms a dimer in the crystal and in solution. Structural comparison of E. coli SpeE to its homologs reveals that it has a large and unique substrate-binding cleft that may account for its lower amine substrate specificity. |
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