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| - | | + | #REDIRECT [[5ovz]] This PDB entry is obsolete and replaced by 5ovz |
| - | ==Structure of the PBP NocT in complex with nopaline==
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| - | <StructureSection load='4pox' size='340' side='right'caption='[[4pox]], [[Resolution|resolution]] 2.29Å' scene=''>
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| - | == Structural highlights ==
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| - | <table><tr><td colspan='2'>[[4pox]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Agrfc Agrfc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4POX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4POX 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=15P:POLYETHYLENE+GLYCOL+(N=34)'>15P</scene>, <scene name='pdbligand=2W2:N-[(1S)-4-CARBAMIMIDAMIDO-1-CARBOXYBUTYL]-D-GLUTAMIC+ACID'>2W2</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
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| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4p0i|4p0i]], [[4pow|4pow]], [[4pp0|4pp0]]</td></tr>
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| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nocT, Atu6027, AGR_pTi_67 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=176299 AGRFC])</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=4pox FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pox OCA], [http://pdbe.org/4pox PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4pox RCSB], [http://www.ebi.ac.uk/pdbsum/4pox PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4pox ProSAT]</span></td></tr>
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| - | </table>
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| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | By modifying the nuclear genome of its host, the plant pathogen Agrobacterium tumefaciens induces the development of plant tumours in which it proliferates. The transformed plant tissues accumulate uncommon low molecular weight compounds called opines that are growth substrates for A. tumefaciens. In the pathogen-induced niche (the plant tumour), a selective advantage conferred by opine assimilation has been hypothesized, but not experimentally demonstrated. Here, using genetics and structural biology, we deciphered how the pathogen is able to bind opines and use them to efficiently compete in the plant tumour. We report high resolution X-ray structures of the periplasmic binding protein (PBP) NocT unliganded and liganded with the opine nopaline (a condensation product of arginine and alpha-ketoglurate) and its lactam derivative pyronopaline. NocT exhibited an affinity for pyronopaline (KD of 0.6 microM) greater than that for nopaline (KD of 3.7 microM). Although the binding-mode of the arginine part of nopaline/pyronopaline in NocT resembled that of arginine in other PBPs, affinity measurement by two different techniques showed that NocT did not bind arginine. In contrast, NocT presented specific residues such as M117 to stabilize the bound opines. NocT relatives that exhibit the nopaline/pyronopaline-binding mode were only found in genomes of the genus Agrobacterium. Transcriptomics and reverse genetics revealed that A. tumefaciens uses the same pathway for assimilating nopaline and pyronopaline. Fitness measurements showed that NocT is required for a competitive colonization of the plant tumour by A. tumefaciens. Moreover, even though the Ti-plasmid conjugal transfer was not regulated by nopaline, the competitive advantage gained by the nopaline-assimilating Ti-plasmid donors led to a preferential horizontal propagation of this Ti-plasmid amongst the agrobacteria colonizing the plant-tumour niche. This work provided structural and genetic evidences to support the niche construction paradigm in bacterial pathogens.
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| - | Agrobacterium uses a unique ligand-binding mode for trapping opines and acquiring a competitive advantage in the niche construction on plant host.,Lang J, Vigouroux A, Planamente S, El Sahili A, Blin P, Aumont-Nicaise M, Dessaux Y, Morera S, Faure D PLoS Pathog. 2014 Oct 9;10(10):e1004444. doi: 10.1371/journal.ppat.1004444., eCollection 2014 Oct. PMID:25299655<ref>PMID:25299655</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 4pox" style="background-color:#fffaf0;"></div>
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| - | == References ==
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| - | <references/>
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| - | __TOC__
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| - | </StructureSection>
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| - | [[Category: Agrfc]]
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| - | [[Category: Large Structures]]
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| - | [[Category: Morera, S]]
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| - | [[Category: Vigouroux, A]]
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| - | [[Category: Class f]]
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| - | [[Category: Pbp]]
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| - | [[Category: Transport protein]]
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