2009
DOI: 10.1016/j.jmb.2008.08.042
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Structure of Selenophosphate Synthetase Essential for Selenium Incorporation into Proteins and RNAs

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Cited by 42 publications
(70 citation statements)
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“…Therefore, homodecamerization, and consequently, the Ser-Sec conversion and selenoprotein biosynthesis, is dependent on the N-terminal region (or N terminus), as we observed by functional complementation with the N-terminally truncated E. coli SelA. Similar results from A. aeolicus SelA N-terminal mutants (27) (7,10), to form Sec-tRNA Sec . The SPS dimerization interface is composed of the ␤-sheet domain of each monomer, a common structural characteristic of the PurM protein superfamily (7).…”
Section: Discussionsupporting
confidence: 76%
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“…Therefore, homodecamerization, and consequently, the Ser-Sec conversion and selenoprotein biosynthesis, is dependent on the N-terminal region (or N terminus), as we observed by functional complementation with the N-terminally truncated E. coli SelA. Similar results from A. aeolicus SelA N-terminal mutants (27) (7,10), to form Sec-tRNA Sec . The SPS dimerization interface is composed of the ␤-sheet domain of each monomer, a common structural characteristic of the PurM protein superfamily (7).…”
Section: Discussionsupporting
confidence: 76%
“…In addition, consistent with the SPS crystallographic structures (PDB ID 3U0O) that were previously described, the glycine-rich N-terminal region of SPS was observed to be flexible in solution, showing high levels of deuterium exchange even after low deuterium exposure time. This flexibility allows the formation of the SPS active site on its "closed" form, upon ATP binding, releasing the catalysis product in its "open" form (7,10).…”
Section: Discussionmentioning
confidence: 99%
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