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J Mol Biol. 2011 May 20;408(5):971-86. doi: 10.1016/j.jmb.2011.03.025. Epub 2011 Mar 31.

Crystal structures and enzymatic properties of a triamine/agmatine aminopropyltransferase from Thermus thermophilus.

Author information

1
Department of Molecular Biology, Tokyo University of Pharmacy and Life Science, Tokyo 192-0392, Japan. mioohnuma@rikkyo.ac.jp

Abstract

To maintain functional conformations of DNA and RNA in high-temperature environments, an extremely thermophilic bacterium, Thermus thermophilus, employs a unique polyamine biosynthetic pathway and produces more than 16 types of polyamines. In the thermophile genome, only one spermidine synthase homolog (SpeE) was found and it was shown to be a key enzyme in the pathway. The catalytic assay of the purified enzyme revealed that it utilizes triamines (norspermidine and spermidine) and agmatine as acceptors in its aminopropyl transfer reaction; therefore, the enzyme was denoted as a triamine/agmatine aminopropyltransferase (TAAPT). We determined the crystal structures of the enzyme complexed with and without the aminopropyl group donor S-adenosylmethionine. Despite sequence and structural similarity with spermidine synthases from other organisms, a novel C-terminal β-sheet and differences in the catalytic site were observed. The C-terminal module interacts with the gatekeeping loop and fixes the open conformation of the loop to recognize larger polyamine substrates such as agmatine and spermidine. Additional computational docking studies suggest that the structural differences of the catalytic site also contribute to recognition of the aminopropyl/aminobutyl or guanidium moiety of the substrates of TAAPT. These results explain in part the extraordinarily diverse polyamine spectrum found in T. thermophilus.

PMID:
21458463
DOI:
10.1016/j.jmb.2011.03.025
[Indexed for MEDLINE]

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