1BS1

DETHIOBIOTIN SYNTHETASE COMPLEXED WITH DETHIOBIOTIN, ADP , INORGANIC PHOSPHATE AND MAGNESIUM

1BS1 の概要

• エントリーDOI: 10.2210/pdb1bs1/pdb
• 分子名称: PROTEIN (DETHIOBIOTIN SYNTHETASE), MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: ligase, biotin biosynthesis, aluminum flouride, atp-binding, phosphoryl transfer
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm: P13000
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24819.35

構造登録者

Kaeck, H.,Sandmark, J.,Gibson, K.J.,Schneider, G.,Lindqvist, Y. (登録日: 1998-08-31, 公開日: 1999-01-13, 最終更新日: 2024-02-07)

主引用文献

Kack, H.,Sandmark, J.,Gibson, K.J.,Schneider, G.,Lindqvist, Y.
Crystal structure of two quaternary complexes of dethiobiotin synthetase, enzyme-MgADP-AlF3-diaminopelargonic acid and enzyme-MgADP-dethiobiotin-phosphate; implications for catalysis.
Protein Sci., 7:2560-2566, 1998

PubMed Abstract: The crystal structures of two complexes of dethiobiotin synthetase, enzyme-diaminopelargonic acid-MgADP-AlF3 and enzyme-dethiobiotin-MgADP-Pi, respectively, have been determined to 1.8 A resolution. In dethiobiotin synthetase, AlF3 together with carbamylated diaminopelargonic acid mimics the phosphorylated reaction intermediate rather than the transition state complex for phosphoryl transfer. Observed differences in the binding of substrate, diaminopelargonic acid, and the product, dethiobiotin, suggest considerable displacements of substrate atoms during the ring closure step of the catalytic reaction. In both complexes, two metal ions are observed at the active site, providing evidence for a two-metal mechanism for this enzyme.

PubMed: 9865950

実験手法

X-RAY DIFFRACTION (1.8 Å)