1TJ7

Structure determination and refinement at 2.44 A resolution of Argininosuccinate lyase from E. coli

1TJ7 の概要

• エントリーDOI: 10.2210/pdb1tj7/pdb
• 分子名称: Argininosuccinate lyase, PHOSPHATE ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: argininosuccinate lyase, crystallin, e. coli, fumarase, aspartase, lyase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm : P11447
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 101214.33

構造登録者

Bhaumik, P.,Koski, M.K.,Bergman, U.,Wierenga, R.K. (登録日: 2004-06-03, 公開日: 2004-10-26, 最終更新日: 2023-08-23)

主引用文献

Bhaumik, P.,Koski, M.K.,Bergmann, U.,Wierenga, R.K.
Structure determination and refinement at 2.44 A resolution of argininosuccinate lyase from Escherichia coli.
Acta Crystallogr.,Sect.D, 60:1964-1970, 2004

PubMed Abstract: Escherichia coli argininosuccinate lyase has been crystallized from a highly concentrated sample of purified recombinant alpha-methylacyl-CoA racemase, in which it occurred as a minor impurity. The structure has been solved using molecular replacement at 2.44 A resolution. The enzyme is tetrameric, but in this crystal form there is a dimer in the asymmetric unit. The tetramer has four active sites; each active site is constructed from loops of three different subunits. One of these catalytic loops, near residues Ser277 and Ser278, was disordered in previous structures of active lyases, but is very well ordered in this structure in one of the subunits owing to the presence of two phosphate ions in the active-site cavity. The positions of these phosphate ions indicate a plausible mode of binding of the succinate moiety of the substrate in the competent catalytic complex.

PubMed: 15502303
DOI: 10.1107/S0907444904021912

実験手法

X-RAY DIFFRACTION (2.44 Å)