1AW8

PYRUVOYL DEPENDENT ASPARTATE DECARBOXYLASE

1AW8 の概要

• エントリーDOI: 10.2210/pdb1aw8/pdb
• 分子名称: L-ASPARTATE-ALPHA-DECARBOXYLASE (3 entities in total)
• 機能のキーワード: decarboxylase, pantothenate pathway, lyase, protein self-processing
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Cytoplasm : P0A790 P0A790
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 25428.64

構造登録者

Albert, A.,Dhanaraj, V.,Genschel, U.,Khan, G.,Ramjee, M.K.,Pulido, R.,Sybanda, B.L.,von Delf, F.,Witty, M.,Blundell, T.L.,Smith, A.G.,Abell, C. (登録日: 1997-10-12, 公開日: 1998-04-29, 最終更新日: 2024-10-23)

主引用文献

Albert, A.,Dhanaraj, V.,Genschel, U.,Khan, G.,Ramjee, M.K.,Pulido, R.,Sibanda, B.L.,von Delft, F.,Witty, M.,Blundell, T.L.,Smith, A.G.,Abell, C.
Crystal structure of aspartate decarboxylase at 2.2 A resolution provides evidence for an ester in protein self-processing.
Nat.Struct.Biol., 5:289-293, 1998

PubMed Abstract: The structure of L-aspartate-alpha-decarboxylase from E. coli has been determined at 2.2 A resolution. The enzyme is a tetramer with pseudofour-fold rotational symmetry. The subunits are six-stranded beta-barrels capped by small alpha-helices at each end. The active sites are located between adjacent subunits. The electron density provides evidence for catalytic pyruvoyl groups at three active sites and an ester at the fourth. The ester is an intermediate in the autocatalytic self-processing leading to formation of the pyruvoyl group. This unprecedented structure provides novel insights into the general phenomenon of protein processing.

PubMed: 9546220
DOI: 10.1038/nsb0498-289

実験手法

X-RAY DIFFRACTION (2.2 Å)