6QWU

4'-phosphopantetheinyl transferase PptAb from Mycobacterium abscessus at pH 5.5 with Mn2+ and CoA.

6QWU の概要

• エントリーDOI: 10.2210/pdb6qwu/pdb
• 関連するPDBエントリー: 6QXQ 6QXR 6QYF 6QYG 6RCX
• 分子名称: Possible 4'-phosphopantetheinyl transferase, COENZYME A, MANGANESE (II) ION, ... (6 entities in total)
• 機能のキーワード: transferase
• 由来する生物種: Mycobacteroides abscessus ATCC 19977
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 26438.58

構造登録者

Nguyen, M.C.,Mourey, L.,Pedelacq, J.D. (登録日: 2019-03-06, 公開日: 2020-03-25, 最終更新日: 2024-01-24)

主引用文献

Nguyen, M.C.,Saurel, O.,Carivenc, C.,Gavalda, S.,Saitta, S.,Tran, M.P.,Milon, A.,Chalut, C.,Guilhot, C.,Mourey, L.,Pedelacq, J.D.
Conformational flexibility of coenzyme A and its impact on the post-translational modification of acyl carrier proteins by 4'-phosphopantetheinyl transferases.
Febs J., 287:4729-4746, 2020

PubMed Abstract: One central question surrounding the biosynthesis of fatty acids and polyketide-derived natural products is how the 4'-phosphopantetheinyl transferase (PPTase) interrogates the essential acyl carrier protein (ACP) domain to fulfill the initial activation step. The triggering factor of this study was the lack of structural information on PPTases at physiological pH, which could bias our comprehension of the mechanism of action of these important enzymes. Structural and functional studies on the family II PPTase PptAb of Mycobacterium abscessus show that pH has a profound effect on the coordination of metal ions and on the conformation of endogenously bound coenzyme A (CoA). The observed conformational flexibility of CoA at physiological pH is accompanied by a disordered 4'-phosphopantetheine (Ppant) moiety. Finally, structural and dynamical information on an isolated mycobacterial ACP domain, in its apo form and in complex with the activator PptAb, suggests an alternate mechanism for the post-translational modification of modular megasynthases.

PubMed: 32128972
DOI: 10.1111/febs.15273

実験手法

X-RAY DIFFRACTION (1.4 Å)