2zau
From Proteopedia
Crystal structure of an N-terminally truncated selenophosphate synthetase from Aquifex aeolicus
Structural highlights
FunctionSELD_AQUAE Synthesizes selenophosphate from selenide and ATP (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedSelenophosphate 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). Structure of an N-terminally truncated selenophosphate synthetase from Aquifex aeolicus.,Matsumoto E, Sekine SI, Akasaka R, Otta Y, Katsura K, Inoue M, Kaminishi T, Terada T, Shirouzu M, Yokoyama S Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Jun 1;64(Pt, 6):453-8. Epub 2008 May 16. PMID:18540050[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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