4RNJ

PaMorA phosphodiesterase domain, apo form

4RNJ の概要

• エントリーDOI: 10.2210/pdb4rnj/pdb
• 関連するPDBエントリー: 4RNF 4RNH 4RNI
• 分子名称: Motility regulator (2 entities in total)
• 機能のキーワード: eal domain, phosphodiesterase, c-di-gmp, hydrolase
• 由来する生物種: Pseudomonas aeruginosa PAO1
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 63454.64

構造登録者

Phippen, C.W.,Tews, I. (登録日: 2014-10-24, 公開日: 2014-11-19, 最終更新日: 2023-09-20)

主引用文献

Phippen, C.W.,Mikolajek, H.,Schlaefli, H.G.,Keevil, C.W.,Webb, J.S.,Tews, I.
Formation and dimerization of the phosphodiesterase active site of the Pseudomonas aeruginosa MorA, a bi-functional c-di-GMP regulator.
Febs Lett., 588:4631-4636, 2014

PubMed Abstract: Diguanylate cyclases (DGC) and phosphodiesterases (PDE), respectively synthesise and hydrolyse the secondary messenger cyclic dimeric GMP (c-di-GMP), and both activities are often found in a single protein. Intracellular c-di-GMP levels in turn regulate bacterial motility, virulence and biofilm formation. We report the first structure of a tandem DGC-PDE fragment, in which the catalytic domains are shown to be active. Two phosphodiesterase states are distinguished by active site formation. The structures, in the presence or absence of c-di-GMP, suggest that dimerisation and binding pocket formation are linked, with dimerisation being required for catalytic activity. An understanding of PDE activation is important, as biofilm dispersal via c-di-GMP hydrolysis has therapeutic effects on chronic infections.

PubMed: 25447517
DOI: 10.1016/j.febslet.2014.11.002

実験手法

X-RAY DIFFRACTION (2.32 Å)