1ZA2

Structure of wild-type E. coli Aspartate Transcarbamoylase in the presence of CTP, carbamoyl phosphate at 2.50 A resolution

1ZA2 の概要

• エントリーDOI: 10.2210/pdb1za2/pdb
• 関連するPDBエントリー: 1TU0 1ZA1
• 分子名称: Aspartate carbamoyltransferase catalytic chain, Aspartate carbamoyltransferase regulatory chain, SODIUM ION, ... (7 entities in total)
• 機能のキーワード: ordered substrate binding, cooperativity, transferase
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 104645.66

構造登録者

Wang, J.,Stieglitz, K.A.,Cardia, J.P.,Kantrowitz, E.R. (登録日: 2005-04-05, 公開日: 2005-06-07, 最終更新日: 2023-08-23)

主引用文献

Wang, J.,Stieglitz, K.A.,Cardia, J.P.,Kantrowitz, E.R.
Structural basis for ordered substrate binding and cooperativity in aspartate transcarbamoylase
Proc.Natl.Acad.Sci.Usa, 102:8881-8886, 2005

PubMed Abstract: X-ray structures of aspartate transcarbamoylase in the absence and presence of the first substrate carbamoyl phosphate are reported. These two structures in conjunction with in silico docking experiments provide snapshots of critical events in the function of the enzyme. The ordered substrate binding, observed experimentally, can now be structurally explained by a conformational change induced upon the binding of carbamoyl phosphate. This induced fit dramatically alters the electrostatics of the active site, creating a binding pocket for aspartate. Upon aspartate binding, a further change in electrostatics causes a second induced fit, the domain closure. This domain closure acts as a clamp that both facilitates catalysis by approximation and also initiates the global conformational change that manifests homotropic cooperativity.

PubMed: 15951418
DOI: 10.1073/pnas.0503742102

実験手法

X-RAY DIFFRACTION (2.5 Å)