Abstract
AmyR is a stress and virulence associated protein from the plant pathogenic Enterobacteriaceae species Erwinia amylovora, and is a functionally conserved ortholog of YbjN from Escherichia coli. The crystal structure of E. amylovora AmyR reveals a class I type III secretion chaperone-like fold, despite the lack of sequence similarity between these two classes of protein and lacking any evidence of a secretion-associated role. The results indicate that AmyR, and YbjN proteins in general, function through protein-protein interactions without any enzymatic action. The YbjN proteins of Enterobacteriaceae show remarkably low sequence similarity with other members of the YbjN protein family in Eubacteria, yet a high level of structural conservation is observed. Across the YbjN protein family sequence conservation is limited to residues stabilising the protein core and dimerization interface, while interacting regions are only conserved between closely related species. This study presents the first structure of a YbjN protein from Enterobacteriaceae, the most highly divergent and well-studied subgroup of YbjN proteins, and an in-depth sequence and structural analysis of this important but poorly understood protein family.
Highlights
Erwinia amylovora is a Gram-negative plant pathogen that belongs to the Enterobacteriaceae family, which is closely related to other pathogenic Enterobacteria such as Escherichia coli, Yersinia pestis, Salmonella enterica and Shigella flexneri [1]
This study reports the crystal structure of E. amylovora AmyR, the first representative structure of a YbjN protein from an Enterobacteriaceae species, which is the most highly divergent and intensely studied YbjN sub-family
The crystal structure of AmyR substituted with selenomethionine was solved at 2.12 Å resolution by multiple wavelength anomalous diffraction (PDB: 5FRK), and native AmyR was determined at 1.95 Å by molecular replacement (PDB: 5FR7) using the selenomethionine structure as a search model
Summary
Erwinia amylovora is a Gram-negative plant pathogen that belongs to the Enterobacteriaceae family, which is closely related to other pathogenic Enterobacteria such as Escherichia coli, Yersinia pestis, Salmonella enterica and Shigella flexneri [1]. The crystal structure of Erwinia amylovora AmyR provides new evidence on the role the YbjN family proteins genomics approach for the study of the virulence and pathogenesis of Erwinia amylovora” from the Autonomous Province of Bolzano and the grant: “GenSelEa” from the Faculty of Science and Technology, Free University of Bolzano. The above mentioned funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript." The funder Diamond Light Source Ltd. provided beamtime at the beamlines I04 and I04-1 for data collection, and support in the form of salaries for the authors DB and MAW but did not have any additional role in the study design, data analysis, decision to publish, or preparation of the manuscript. The specific roles of these authors are articulated in the ‘author contributions’ section
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