1I5O

CRYSTAL STRUCTURE OF MUTANT R105A OF E. COLI ASPARTATE TRANSCARBAMOYLASE

1I5O の概要

• エントリーDOI: 10.2210/pdb1i5o/pdb
• 関連するPDBエントリー: 5at1 6at1
• 分子名称: ASPARTATE TRANSCARBAMOYLASE CATALYTIC CHAIN, ASPARTATE TRANSCARBAMOYLASE REGULATORY CHAIN, ZINC ION, ... (5 entities in total)
• 機能のキーワード: mutant aspartate transcarbamoylase, t-state, pala at the regulatory site, 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: 103175.17

構造登録者

Macol, C.P.,Tsuruta, H.,Stec, B.,Kantrowitz, E.R. (登録日: 2001-02-28, 公開日: 2001-05-02, 最終更新日: 2023-08-09)

主引用文献

Macol, C.P.,Tsuruta, H.,Stec, B.,Kantrowitz, E.R.
Direct structural evidence for a concerted allosteric transition in Escherichia coli aspartate transcarbamoylase.
Nat.Struct.Biol., 8:423-426, 2001

PubMed Abstract: Regulation of protein function, often achieved by allosteric mechanisms, is central to normal physiology and cellular processes. Although numerous models have been proposed to account for the cooperative binding of ligands to allosteric proteins and enzymes, direct structural support has been lacking. Here, we used a combination of X-ray crystallography and small angle X-ray scattering in solution to provide direct structural evidence that the binding of ligand to just one of the six active sites of Escherichia coli aspartate transcarbamoylase induces a concerted structural transition from the T to the R state.

PubMed: 11323717
DOI: 10.1038/87582

実験手法

X-RAY DIFFRACTION (2.8 Å)