4pp0: Difference between revisions

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==Structure of the PBP NocT-M117N in complex with pyronopaline==
==Structure of the PBP NocT-M117N in complex with pyronopaline==
<StructureSection load='4pp0' size='340' side='right' caption='[[4pp0]], [[Resolution|resolution]] 1.57&Aring;' scene=''>
<StructureSection load='4pp0' size='340' side='right'caption='[[4pp0]], [[Resolution|resolution]] 1.57&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4pp0]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PP0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PP0 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4pp0]] 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=4PP0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PP0 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=OP1:1-[(1S)-4-CARBAMIMIDAMIDO-1-CARBOXYBUTYL]-5-OXO-D-PROLINE'>OP1</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=OP1:1-[(1S)-4-CARBAMIMIDAMIDO-1-CARBOXYBUTYL]-5-OXO-D-PROLINE'>OP1</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4p0i|4p0i]], [[4pow|4pow]], [[4pox|4pox]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4p0i|4p0i]], [[4pow|4pow]], [[4pox|4pox]]</td></tr>
<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>
<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=4pp0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pp0 OCA], [http://pdbe.org/4pp0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4pp0 RCSB], [http://www.ebi.ac.uk/pdbsum/4pp0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4pp0 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=4pp0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pp0 OCA], [http://pdbe.org/4pp0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4pp0 RCSB], [http://www.ebi.ac.uk/pdbsum/4pp0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4pp0 ProSAT]</span></td></tr>
</table>
</table>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Agrfc]]
[[Category: Large Structures]]
[[Category: Morera, S]]
[[Category: Morera, S]]
[[Category: Vigouroux, A]]
[[Category: Vigouroux, A]]

Revision as of 10:33, 17 April 2019

Structure of the PBP NocT-M117N in complex with pyronopalineStructure of the PBP NocT-M117N in complex with pyronopaline

Structural highlights

4pp0 is a 2 chain structure with sequence from Agrfc. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
Gene:nocT, Atu6027, AGR_pTi_67 (AGRFC)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

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.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Lang J, Vigouroux A, Planamente S, El Sahili A, Blin P, Aumont-Nicaise M, Dessaux Y, Morera S, Faure D. Agrobacterium uses a unique ligand-binding mode for trapping opines and acquiring a competitive advantage in the niche construction on plant host. PLoS Pathog. 2014 Oct 9;10(10):e1004444. doi: 10.1371/journal.ppat.1004444., eCollection 2014 Oct. PMID:25299655 doi:http://dx.doi.org/10.1371/journal.ppat.1004444

4pp0, resolution 1.57Å

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