Structural and dynamical properties of the autotransporter esterase EstA from bacterium Pseudomonas aeruginosa were studied using molecular dynamics (MD) simulations. Four different systems, including the full-length EstA enzyme inserted into a solvated 1-palmitoyl-2-oleoyl-phosphatidylethanolamine (POPE) lipid bilayer, as well as the solvated isolated passenger domain of EstA were simulated without ligand and in complex with 4-hydroxyphenyloctanoate bound as tetrahedral intermediate. Detailed analysis of non-covalent interactions was performed based on 100 ns long MD simulations. It was found that active site interactions include not only the catalytic triad (Ser14, Asp286, His289), but also a three-residue oxyanion hole (backbone of Ser14, Gly92 and Asn147), hydrophobic residues involved in tetrahedral intermediate stabilisation, and residues participating in the active site hydrogen bond network. Moreover, interactions between protein domains were analysed and it was found that interacting residues are located on specific structures not usually found in GDSL hydrolases or autotransporter β barrels. In the case of full-length EstA enzyme, MD simulations point to specific interactions between the central and remote regions of the active site which are important for adequate intermediate stabilisation.

铜绿假单胞菌自转运蛋白酯酶EstA的结构和动力学性质使用分子动力学（MD）模拟进行了研究。模拟了四个不同的系统，包括全长的EstA酶插入溶剂化的1-棕榈酰基-2-油酰基-磷脂酰乙醇胺（POPE）脂质双层中，以及没有配体且与4-羟基苯基辛酸酯作为四面体中间体结合。对非共价相互作用的详细分析是基于100 ns长的MD模拟进行的。发现活性位点相互作用不仅包括催化三联体（Ser14，Asp286，His289），而且还包括三个残基的氧阴离子孔（Ser14，Gly92和Asn147的骨架），参与四面体中间稳定作用的疏水残基以及参与的残基。在活性位点的氢键网络中。此外，分析了蛋白质结构域之间的相互作用，发现相互作用残基位于通常在GDSL水解酶或自转运β桶中不常见的特定结构上。在全长EstA酶的情况下，MD模拟指出了活性位点中心区域和远端区域之间的特定相互作用，这对于适当的中间稳定化非常重要。