4E2F

Crystal Structure of E. coli Aspartate Transcarbamoylase K164E/E239K Mutant in an intermediate state

4E2F の概要

• エントリーDOI: 10.2210/pdb4e2f/pdb
• 関連するPDBエントリー: 1D09 1ZA1
• 分子名称: Aspartate carbamoyltransferase catalytic chain, Aspartate carbamoyltransferase regulatory chain, ZINC ION, ... (4 entities in total)
• 機能のキーワード: transferase, cooperativity, allosteric transition, intermediate, transferase-protein binding complex, transferase/protein binding
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 309276.83

構造登録者

Guo, W.,Kantrowitz, E.R. (登録日: 2012-03-08, 公開日: 2012-05-02, 最終更新日: 2024-02-28)

主引用文献

Guo, W.,West, J.M.,Dutton, A.S.,Tsuruta, H.,Kantrowitz, E.R.
Trapping and structure determination of an intermediate in the allosteric transition of aspartate transcarbamoylase.
Proc.Natl.Acad.Sci.USA, 109:7741-7746, 2012

PubMed Abstract: X-ray crystallography and small-angle X-ray scattering (SAXS) in solution have been used to show that a mutant aspartate transcarbamoylase exists in an intermediate quaternary structure between the canonical T and R structures. Additionally, the SAXS data indicate a pH-dependent structural alteration consistent with either a pH-induced conformational change or a pH-induced alteration in the T to R equilibrium. These data indicate that this mutant is not a model for the R state, as has been proposed, but rather represents the enzyme trapped along the path of the allosteric transition between the T and R states.

PubMed: 22547808
DOI: 10.1073/pnas.1119683109

実験手法

X-RAY DIFFRACTION (2.8 Å)