| Literature DB >> 18540050 |
Eiko Matsumoto1, Shun Ichi Sekine, Ryogo Akasaka, Yumi Otta, Kazushige Katsura, Mio Inoue, Tatsuya Kaminishi, Takaho Terada, Mikako Shirouzu, Shigeyuki Yokoyama.
Abstract
Selenophosphate synthetase (SPS) catalyzes the activation of selenide with ATP to synthesize selenophosphate, the reactive selenium donor for biosyntheses of both the 21st amino acid selenocysteine and 2-selenouridine nucleotides in tRNA anticodons. The crystal structure of an N-terminally (25 residues) truncated fragment of SPS (SPS-DeltaN) from Aquifex aeolicus has been determined at 2.0 A resolution. The structure revealed SPS to be a two-domain alpha/beta protein, with domain folds that are homologous to those of PurM-superfamily proteins. In the crystal, six monomers of SPS-DeltaN form a hexamer of 204 kDa, whereas the molecular weight estimated by ultracentrifugation was approximately 63 kDa, which is comparable to the calculated weight of the dimer (68 kDa).Entities:
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Year: 2008 PMID: 18540050 PMCID: PMC2496870 DOI: 10.1107/S1744309108012074
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN: 1744-3091