The aim of this work has been the structural and functional study of a putative carboxylesterase purified from P. aeruginosa, namely PA3859. The protein has been purified from the wild type and a preliminary biochemical charcterization was carried out. The PA3859 gene was then cloned and the recombinant protein was expressed in E. coli (Chapter 2). The recombinant PA3859 was successfully crystallized and its 3D crystal structure was determined (Chapter 3 and 4). Starting from the enzyme 3D structure, an approach involving in silico, in vitro and in vivo assays lead to the reliable determination of the PA3859 physiological function (Chapter 5, 6, 7).
Pseudomonas aeruginosa PA3859: From Structure to Function
Pesaresi, Alessandro
2005
Abstract
The aim of this work has been the structural and functional study of a putative carboxylesterase purified from P. aeruginosa, namely PA3859. The protein has been purified from the wild type and a preliminary biochemical charcterization was carried out. The PA3859 gene was then cloned and the recombinant protein was expressed in E. coli (Chapter 2). The recombinant PA3859 was successfully crystallized and its 3D crystal structure was determined (Chapter 3 and 4). Starting from the enzyme 3D structure, an approach involving in silico, in vitro and in vivo assays lead to the reliable determination of the PA3859 physiological function (Chapter 5, 6, 7).File | Dimensione | Formato | |
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https://hdl.handle.net/20.500.14242/105453
URN:NBN:IT:SISSA-105453