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TitleDimer-Dimer Interaction of the Bacterial Selenocysteine Synthase SelA Promotes Functional Active-Site Formation and Catalytic Specificity
Journal, issue, pagesJ. Mol. Biol., Vol. 426, Page 1723-1735, Year 2014
Publish dateMay 29, 2013 (structure data deposition date)
AuthorsItoh, Y. / Brocker, M.J. / Sekine, S. / Soll, D. / Yokoyama, S.
External linksJ. Mol. Biol. / PubMed:24456689
MethodsX-ray diffraction
Resolution2.4 - 3.35 Å
Structure data

PDB-3wcn:
Crystal structure of the depentamerized mutant of selenocysteine synthase SelA
Method: X-RAY DIFFRACTION / Resolution: 3.35 Å

PDB-3wco:
Crystal structure of the depentamerized mutant of N-terminal truncated selenocysteine synthase SelA
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

Chemicals

ChemComp-THJ:
THIOSULFATE

ChemComp-HOH:
WATER

Source
  • aquifex aeolicus (bacteria)
KeywordsTRANSFERASE / Fold-type-I pyridoxal 5'-phosphate (PLP) dependent enzyme / L-seryl-tRNA(Sec) selenium transferase / selenocysteine synthesis / selenium metabolism / homodimer

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