3X1K

crystal structure of Phosphoapantetheine adenylyltransferase PPAT/CoaD with AMP-PNP from Pseudomonas aerugonosa

3X1K の概要

• エントリーDOI: 10.2210/pdb3x1k/pdb
• 関連するPDBエントリー: 3X1J 3X1M 4RUK
• 分子名称: Phosphopantetheine adenylyltransferase, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, DIMETHYL SULFOXIDE, ... (7 entities in total)
• 機能のキーワード: rossmann fold, transferase
• 由来する生物種: Pseudomonas aeruginosa 2192
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 111710.42

構造登録者

Chatterjee, R.,Datta, S. (登録日: 2014-11-20, 公開日: 2015-11-25, 最終更新日: 2023-11-08)

主引用文献

Chatterjee, R.,Mondal, A.,Basu, A.,Datta, S.
Transition of phosphopantetheine adenylyltransferase from catalytic to allosteric state is characterized by ternary complex formation in Pseudomonas aeruginosa
Biochim.Biophys.Acta, 1864:773-786, 2016

PubMed Abstract: Phosphopantetheine adenylyltransferase (PPAT) is a rate limiting enzyme which catalyzes the conversion of ATP and pantetheine to dephosphocoenzyme and pyrophosphate. The enzyme is allosteric in nature and regulated by Coenzyme A (CoA) through feedback inhibition. So far, several structures have been solved to decipher the catalytic mechanism of this enzyme.

PubMed: 27041211
DOI: 10.1016/j.bbapap.2016.03.018

実験手法

X-RAY DIFFRACTION (2.547 Å)