4AFY

Crystal structure of the FimX EAL domain in complex with reaction product pGpG

4AFY の概要

• エントリーDOI: 10.2210/pdb4afy/pdb
• 分子名称: FIMX, 5'-R(*GP*GP)-3', MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: hydrolase, cdigmp biofilm, phosphodiesterase
• 由来する生物種: PSEUDOMONAS AERUGINOSA PAO1; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 61974.59

構造登録者

Robert-Paganin, J.,Nonin-Lecomte, S.,Rety, S. (登録日: 2012-01-23, 公開日: 2013-01-09, 最終更新日: 2023-12-20)

主引用文献

Robert-Paganin, J.,Nonin-Lecomte, S.,Rety, S.
Crystal Structure of an Eal Domain in Complex with Reaction Product 5'-Pgpg
Plos One, 7:52424-, 2012

PubMed Abstract: FimX is a large multidomain protein containing an EAL domain and involved in twitching motility in Pseudomonas aeruginosa. We present here two crystallographic structures of the EAL domain of FimX (residues 438-686): one of the apo form and the other of a complex with 5'-pGpG, the reaction product of the hydrolysis of c-di-GMP. In both crystal forms, the EAL domains form a dimer delimiting a large cavity encompassing the catalytic pockets. The ligand is trapped in this cavity by its sugar phosphate moiety. We confirmed by NMR that the guanine bases are not involved in the interaction in solution. We solved here the first structure of an EAL domain bound to the reaction product 5'-pGpG. Though isolated FimX EAL domain has a very low catalytic activity, which would not be significant compared to other catalytic EAL domains, the structure with the product of the reaction can provides some hints in the mechanism of hydrolysis of the c-di-GMP by EAL domains.

PubMed: 23285035
DOI: 10.1371/JOURNAL.PONE.0052424

実験手法

X-RAY DIFFRACTION (2.01 Å)