Cloning, purification, crystallization and 1.57 Å resolution X‐ray data analysis of AmsI, the tyrosine phosphatase controlling amylovoran biosynthesis in the plant pathogen Erwinia amylovora. Issue 12 (1st December 2014)

• Record Type: Journal Article
• Authors: Benini, Stefano; Caputi, Lorenzo; Cianci, Michele
• Is Part Of: Acta crystallographica. Volume 70:Issue 12(2014:Dec.)
• Page Start: 1693
• Page End: 1696
• Publication Date: 2014-12-01
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X14024947
• Languages: English
• ISSNs: 2053-230X

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>The Gram‐negative bacterium <italic>Erwinia amylovora</italic> is a destructive pathogen of plants belonging to the Rosaceae family. Amongst its pathogenicity factors, <italic>E. amylovora</italic> produces the exopolysaccharide amylovoran, which contributes to the occlusion of plant vessels, causing wilting of shoots and eventually resulting in plant death. Amylovoran biosynthesis requires the presence of 12 genes (from <italic>ams</italic>A to <italic>ams</italic>L) clustered in the <italic>ams</italic> region of the <italic>E. amylovora</italic> genome. They mostly encode glycosyl transferases (AmsG, AmsB, AmsD, AmsE, AmsJ and AmsK), proteins involved in amylovoran translocation and assembly (AmsH, AmsL and AmsC), and also a tyrosine kinase (AmsA) and a tyrosine phosphatase (AmsI), which are both involved in the regulation of amylovoran biosynthesis. The low‐molecular‐weight protein tyrosine phosphatase AmsI was overexpressed as a His₆‐tagged protein in <italic>Escherichia coli</italic>, purified and crystallized. X‐ray diffraction data were collected to a maximum resolution of 1.57 Å in space group <italic>P</italic>3₁21.</p> </abstract>