View source for 5um2


==Functional and structural characterization of a Sulfate-binding protein (Sbp) from Xanthomonas citri==
<StructureSection load='5um2' size='340' side='right'caption='[[5um2]], [[Resolution|resolution]] 1.14&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
<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>
== Function ==
[https://www.uniprot.org/uniprot/Q8PNN7_XANAC Q8PNN7_XANAC] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.

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>
</div>
<div class="pdbe-citations 5um2" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Xanthomonas citri pv. citri str. 306]]
[[Category: Balan A]]
[[Category: Hyvonen M]]
[[Category: Pereira CT]]