5UM2

Functional and structural characterization of a Sulfate-binding protein (Sbp) from Xanthomonas citri

Summary for 5UM2

• Entry DOI: 10.2210/pdb5um2/pdb
• Descriptor: ABC transporter sulfate binding protein, SULFATE ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: abc transporter, periplasmic domain, transport protein
• Biological source: Xanthomonas axonopodis pv. citri
• Total number of polymer chains: 1
• Total formula weight: 37748.31

Authors

Pereira, C.T.,Hyvonen, M.,Balan, A. (deposition date: 2017-01-26, release date: 2017-03-29, Last modification date: 2023-10-04)

Primary citation

Pereira, C.T.,Roesler, C.,Faria, J.N.,Fessel, M.R.,Balan, A.
Sulfate-Binding Protein (Sbp) from Xanthomonas citri: Structure and Functional Insights.
Mol. Plant Microbe Interact., 30:578-588, 2017

PubMed Abstract: The uptake and transport of sulfate in bacteria is mediated by an ATP-binding cassette transporter (ABC transporter) encoded by sbpcysUWA genes, whose importance has been widely demonstrated due to their relevance in cysteine synthesis and bacterial growth. In Xanthomonas citri, the causative agent of canker disease, the expression of components from this ABC transporter and others related to uptake of organic sulfur sources has been shown during in vitro growth cultures. In this work, based on gene reporter and proteomics analyses, we showed the activation of the promoter that controls the sbpcysUWA operon in vitro and in vivo and the expression of sulfate-binding protein (Sbp), a periplasmic-binding protein, indicating that this protein plays an important function during growth and that the transport system is active during Citrus sinensis infection. To characterize Sbp, we solved its three-dimensional structure bound to sulfate at 1.14 Å resolution and performed biochemical and functional characterization. The results revealed that Sbp interacts with sulfate without structural changes, but the interaction induces a significant increasing of protein thermal stability. Altogether, the results presented in this study show the evidence of the functionality of the ABC transporter for sulfate in X. citri and its relevance during infection.

PubMed: 28562158
DOI: 10.1094/MPMI-02-17-0032-R

Experimental method

X-RAY DIFFRACTION (1.14 Å)