4d74
1.57 A crystal structure of erwinia amylovora tyrosine phosphatase amsI1.57 A crystal structure of erwinia amylovora tyrosine phosphatase amsI
Structural highlights
Function[AMSI_ERWAM] May function as a phosphatase required for amylovoran (an exopolysaccharide that functions as a virulence factor) production. Publication Abstract from PubMedThe Gram-negative bacterium Erwinia amylovora is a destructive pathogen of plants belonging to the Rosaceae family. Amongst its pathogenicity factors, E. amylovora 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 amsA to amsL) clustered in the ams region of the E. amylovora 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 Escherichia coli, purified and crystallized. X-ray diffraction data were collected to a maximum resolution of 1.57 A in space group P3121. Cloning, purification, crystallization and 1.57 A resolution X-ray data analysis of AmsI, the tyrosine phosphatase controlling amylovoran biosynthesis in the plant pathogen Erwinia amylovora.,Benini S, Caputi L, Cianci M Acta Crystallogr F Struct Biol Commun. 2014 Dec 1;70(Pt 12):1693-6. doi:, 10.1107/S2053230X14024947. Epub 2014 Nov 28. PMID:25484228[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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