5ub6: Difference between revisions

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<StructureSection load='5ub6' size='340' side='right'caption='[[5ub6]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='5ub6' size='340' side='right'caption='[[5ub6]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5ub6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Xanac Xanac]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UB6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UB6 FirstGlance]. <br>
<table><tr><td colspan='2'>[[5ub6]] is a 2 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=5UB6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UB6 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ub3|5ub3]], [[5ub4|5ub4]], [[5ub7|5ub7]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">XAC2383 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=190486 XANAC])</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=5ub6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ub6 OCA], [https://pdbe.org/5ub6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ub6 RCSB], [https://www.ebi.ac.uk/pdbsum/5ub6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ub6 ProSAT]</span></td></tr>
<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=5ub6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ub6 OCA], [http://pdbe.org/5ub6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ub6 RCSB], [http://www.ebi.ac.uk/pdbsum/5ub6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ub6 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/Q8PJZ4_XANAC Q8PJZ4_XANAC]
The second messenger cyclic diguanylate monophosphate (c-di-GMP) is a central regulator of bacterial lifestyle, controlling several behaviors, including the switch between sessile and motile states. The c-di-GMP levels are controlled by the interplay between diguanylate cyclases (DGCs) and phosphodiesterases, which synthesize and hydrolyze this second messenger, respectively. These enzymes often contain additional domains that regulate activity via binding of small molecules, covalent modification, or protein-protein interactions. A major challenge remains to understand how DGC activity is regulated by these additional domains or interaction partners in specific signaling pathways. Here, we identified a pair of co-transcribed genes (xac2382 and xac2383) in the phytopathogenic, Gram-negative bacterium Xanthomonas citri subsp. citri (Xac), whose mutations resulted in opposing motility phenotypes. We show that the periplasmic cache domain of XAC2382, a membrane-associated DGC, interacts with XAC2383, a periplasmic binding protein, and we provide evidence that this interaction regulates XAC2382 DGC activity. Moreover, we solved the crystal structure of XAC2383 with different ligands, indicating a preference for negatively charged phosphate-containing compounds. We propose that XAC2383 acts as a periplasmic sensor that, upon binding its ligand, inhibits the DGC activity of XAC2382. Of note, we also found that this previously uncharacterized signal transduction system is present in several other bacterial phyla, including Gram-positive bacteria. Phylogenetic analysis of homologs of the XAC2382-XAC2383 pair supports several independent origins that created new combinations of XAC2382 homologs with a conserved periplasmic cache domain with different cytoplasmic output module architectures.
 
A bipartite periplasmic receptor-diguanylate cyclase pair (XAC2383-XAC2382) in the bacterium Xanthomonas citri.,Teixeira RD, Guzzo CR, Arevalo SJ, Andrade MO, Abrahao J, de Souza RF, Farah CS J Biol Chem. 2018 Jul 6;293(27):10767-10781. doi: 10.1074/jbc.RA118.003475. Epub , 2018 May 4. PMID:29728456<ref>PMID:29728456</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5ub6" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Phosphate-binding protein|Phosphate-binding protein]]
*[[Phosphate-binding protein|Phosphate-binding protein]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Xanac]]
[[Category: Xanthomonas citri pv. citri str. 306]]
[[Category: Farah, C S]]
[[Category: Farah CS]]
[[Category: Guzzo, C R]]
[[Category: Guzzo CR]]
[[Category: Teixeira, R D]]
[[Category: Teixeira RD]]
[[Category: Metal binding protein]]
[[Category: Periplasmic binding protein periplasmic sensor pyrophosphate phosphonate-bd]]

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