5MFU

PA3825-EAL Mn-pGpG Structure

5MFU の概要

• エントリーDOI: 10.2210/pdb5mfu/pdb
• 関連するPDBエントリー: 4Y8E 4Y9M 4Y9N 4Y9O 4Y9P 4Y9Q 5M1T 5MF5
• 分子名称: cyclic-guanylate-specific phosphodiesterase, RNA (pGpG), MANGANESE (II) ION, ... (5 entities in total)
• 機能のキーワード: eal, phosphodiesterase, biofilm formation, p aeruginosa, pa3825, hydrolase
• 由来する生物種: Pseudomonas aeruginosa; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 28948.63

構造登録者

Horrell, S.,Bellini, D.,Strange, R.,Wagner, A.,Walsh, M. (登録日: 2016-11-18, 公開日: 2017-03-01, 最終更新日: 2025-12-17)

主引用文献

Bellini, D.,Horrell, S.,Hutchin, A.,Phippen, C.W.,Strange, R.W.,Cai, Y.,Wagner, A.,Webb, J.S.,Tews, I.,Walsh, M.A.
Dimerisation induced formation of the active site and the identification of three metal sites in EAL-phosphodiesterases.
Sci Rep, 7:42166-42166, 2017

PubMed Abstract: The bacterial second messenger cyclic di-3',5'-guanosine monophosphate (c-di-GMP) is a key regulator of bacterial motility and virulence. As high levels of c-di-GMP are associated with the biofilm lifestyle, c-di-GMP hydrolysing phosphodiesterases (PDEs) have been identified as key targets to aid development of novel strategies to treat chronic infection by exploiting biofilm dispersal. We have studied the EAL signature motif-containing phosphodiesterase domains from the Pseudomonas aeruginosa proteins PA3825 (PA3825) and PA1727 (MucR). Different dimerisation interfaces allow us to identify interface independent principles of enzyme regulation. Unlike previously characterised two-metal binding EAL-phosphodiesterases, PA3825 in complex with pGpG provides a model for a third metal site. The third metal is positioned to stabilise the negative charge of the 5'-phosphate, and thus three metals could be required for catalysis in analogy to other nucleases. This newly uncovered variation in metal coordination may provide a further level of bacterial PDE regulation.

PubMed: 28186120
DOI: 10.1038/srep42166

実験手法

X-RAY DIFFRACTION (2.15 Å)