2ZAU

Crystal structure of an N-terminally truncated selenophosphate synthetase from Aquifex aeolicus

Summary for 2ZAU

• Entry DOI: 10.2210/pdb2zau/pdb
• Related: 2YYE 2ZOD
• Descriptor: Selenide, water dikinase, PHOSPHATE ION (3 entities in total)
• Functional Keywords: intramolecular s-s bond, trimer of dimers, atp-binding, kinase, magnesium, nucleotide-binding, selenium, selenocysteine, transferase, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi
• Biological source: Aquifex aeolicus
• Total number of polymer chains: 3
• Total formula weight: 103075.04

Authors

Sekine, S.,Matsumoto, E.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2007-10-10, release date: 2008-06-17, Last modification date: 2024-10-30)

Primary citation

Matsumoto, E.,Sekine, S.,Akasaka, R.,Otta, Y.,Katsura, K.,Inoue, M.,Kaminishi, T.,Terada, T.,Shirouzu, M.,Yokoyama, S.
Structure of an N-terminally truncated selenophosphate synthetase from Aquifex aeolicus
Acta Crystallogr.,Sect.F, 64:453-458, 2008

PubMed 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).

PubMed: 18540050
DOI: 10.1107/S1744309108012074

Experimental method

X-RAY DIFFRACTION (2 Å)