5um2

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==Functional and structural characterization of a Sulfate-binding protein (Sbp) from Xanthomonas citri==
==Functional and structural characterization of a Sulfate-binding protein (Sbp) from Xanthomonas citri==
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<StructureSection load='5um2' size='340' side='right' caption='[[5um2]], [[Resolution|resolution]] 1.14&Aring;' scene=''>
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<StructureSection load='5um2' size='340' side='right'caption='[[5um2]], [[Resolution|resolution]] 1.14&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5um2]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UM2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UM2 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5um2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Xanthomonas_citri_pv._citri_str._306 Xanthomonas citri pv. citri str. 306]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UM2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UM2 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.14&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5um2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5um2 OCA], [http://pdbe.org/5um2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5um2 RCSB], [http://www.ebi.ac.uk/pdbsum/5um2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5um2 ProSAT]</span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5um2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5um2 OCA], [https://pdbe.org/5um2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5um2 RCSB], [https://www.ebi.ac.uk/pdbsum/5um2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5um2 ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q8PNN7_XANAC Q8PNN7_XANAC]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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BACKGROUND: The Xanthomonas citri pv. citri (X. citri) is a phytopathogenic bacterium that infects different species of citrus plants where it causes canker disease. The adaptation to different habitats is related to the ability of the cells to metabolize and to assimilate diverse compounds, including sulfur, an essential element for all organisms. In Escherichia coli, the necessary sulfur can be obtained by a set of proteins whose genes belong to the cys regulon. Although the cys regulon proteins and their importance have been described in many other bacteria, there are no data related to these proteins in X. citri or in the Xanthomonas genus. The study of the relevance of these systems in these phytopathogenic bacteria that have distinct mechanisms of infection is one essential step toward understanding their physiology. In this work, we used bioinformatics, molecular modeling and transcription analysis (RT-PCR) to identify and characterize the putative cys regulon genes in X. citri. RESULTS: We showed that the ATP Binding Cassette Transporter (ABC transporter) SbpCysUWA for sulfate uptake is conserved in X. citri and translated in presence of sulfate. On the other hand, differently from what is predicted in databases, according molecular modeling and phylogenetic analysis, X. citri does not show a proper taurine transporter, but two different ABC systems related to the alkanesulfonate/sulfonate transport that were recently acquired during evolution. RT-PCR analysis evidenced that these genes and their putative transcriptional regulator CysB are rather transcripted in XAM1, a medium with defined concentration of sulfate, than LB. CONCLUSIONS: The presence of at least three distinct systems for sulfate and sulfonates assimilation in X. citri evidenced the importance of these compounds for the bacterium. The transcription of genes involved with alkanesulfonate/sulfur compounds in XAM1 along to CysB suggests that despite the differences in the transporters, the regulation of these systems might be similar to the described for E. coli. Altogether, these results will serve as a foundation for further studies aimed to understanding the relevance of sulfur in growth, virulence and pathogenesis of X. citri and related bacteria.
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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 A 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.
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The sulfur/sulfonates transport systems in Xanthomonas citri pv. citri.,Pereira CT, Moutran A, Fessel M, Balan A BMC Genomics. 2015 Jul 14;16:524. doi: 10.1186/s12864-015-1736-5. PMID:26169280<ref>PMID:26169280</ref>
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Sulfate-Binding Protein (Sbp) from Xanthomonas citri: Structure and Functional Insights.,Pereira CT, Roesler C, Faria JN, Fessel MR, Balan A Mol Plant Microbe Interact. 2017 Jul;30(7):578-588. doi:, 10.1094/MPMI-02-17-0032-R. Epub 2017 May 31. PMID:28562158<ref>PMID:28562158</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Balan, A]]
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[[Category: Large Structures]]
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[[Category: Hyvonen, M]]
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[[Category: Xanthomonas citri pv. citri str. 306]]
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[[Category: Pereira, C T]]
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[[Category: Balan A]]
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[[Category: Abc transporter]]
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[[Category: Hyvonen M]]
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[[Category: Periplasmic domain]]
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[[Category: Pereira CT]]
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[[Category: Transport protein]]
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Current revision

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

PDB ID 5um2

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