Abstract
Together with genome analysis and knock-out mutants, structural and functional characterization of proteins provide valuable hints on the biology of the organism under investigation. Structural characterization can be achieved by techniques such as X-ray crystallography, NMR, Cryo-EM. The information derived from the structure are a good starting point to comprehend the details of the proteins molecular function for a better understanding of their biological role. This review aims at describing the progress in the structural and functional characterization of proteins from the plant pathogen Erwinia amylovora obtained by structural biology and currently deposited in the Protein Data Bank.
Highlights
Erwinia amylovora, the plant pathogen responsible for the fire blight disease in Rosaceae still causes huge losses in apple and pear orchards worldwide (Vrancken et al 2013)
The siderophore mediated iron uptake system, which scavenges the iron required for the pathogen metabolism from the host (Smits and Duffy 2011)
A series of virulence and pathogenicity factors are necessary for the pathogen to thrive (Borruso et al 2017)
Summary
The plant pathogen responsible for the fire blight disease in Rosaceae still causes huge losses in apple and pear orchards worldwide (Vrancken et al 2013). E. amylovora is one of the top ten plant pathogen for its impact on global apple and pear production (Mansfield et al 2012). The type three secretion system (T3SS), that is necessary to secrete effector proteins and suppress the host organism’s defenses (Vrancken et al 2013). The exopolysaccharide biosynthetic pathway, producing amylovoran and levan, required to protect the bacteria and causing wilting of shoots and blight symptoms (Langlotz et al 2011; Gross et al 1992). The siderophore mediated iron uptake system, which scavenges the iron required for the pathogen metabolism from the host (Smits and Duffy 2011). A series of virulence and pathogenicity factors are necessary for the pathogen to thrive (Borruso et al 2017)
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