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| | <StructureSection load='7nrr' size='340' side='right'caption='[[7nrr]], [[Resolution|resolution]] 1.67Å' scene=''> | | <StructureSection load='7nrr' size='340' side='right'caption='[[7nrr]], [[Resolution|resolution]] 1.67Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[7nrr]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7NRR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7NRR FirstGlance]. <br> | + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7NRR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7NRR FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DHC:CAFFEIC+ACID'>DHC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 1.67Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DHC:CAFFEIC+ACID'>DHC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[7nqg|7nqg]], [[7nr2|7nr2]], [[7nra|7nra]]</div></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=7nrr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7nrr OCA], [https://pdbe.org/7nrr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7nrr RCSB], [https://www.ebi.ac.uk/pdbsum/7nrr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7nrr ProSAT]</span></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=7nrr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7nrr OCA], [https://pdbe.org/7nrr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7nrr RCSB], [https://www.ebi.ac.uk/pdbsum/7nrr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7nrr ProSAT]</span></td></tr> |
| | </table> | | </table> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bisson, C]] | + | [[Category: Bisson C]] |
| - | [[Category: Hitchcock, A]] | + | [[Category: Hitchcock A]] |
| - | [[Category: Kelly, D J]] | + | [[Category: Kelly DJ]] |
| - | [[Category: Rafferty, J B]] | + | [[Category: Rafferty JB]] |
| - | [[Category: Salmon, R C]] | + | [[Category: Salmon RC]] |
| - | [[Category: Thomas, G H]] | + | [[Category: Thomas GH]] |
| - | [[Category: West, L]] | + | [[Category: West L]] |
| - | [[Category: Hydroxycinnamate]]
| + | |
| - | [[Category: Lignin]]
| + | |
| - | [[Category: Solute binding protein]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| - | [[Category: Trap transporter]]
| + | |
| Structural highlights
Publication Abstract from PubMed
The organic polymer lignin is a component of plant cell walls, which like (hemi)-cellulose is highly abundant in nature and relatively resistant to degradation. However, extracellular enzymes released by natural microbial consortia can cleave the beta-aryl ether linkages in lignin, releasing monoaromatic phenylpropanoids that can be further catabolised by diverse species of bacteria. Biodegradation of lignin is therefore important in global carbon cycling, and its natural abundance also makes it an attractive biotechnological feedstock for the industrial production of commodity chemicals. Whilst the pathways for degradation of lignin-derived aromatics have been extensively characterised, much less is understood about how they are recognised and taken up from the environment. The purple phototrophic bacterium Rhodopseudomonas palustris can grow on a range of phenylpropanoid monomers and is a model organism for studying their uptake and breakdown. R. palustris encodes a tripartite ATP-independent periplasmic (TRAP) transporter (TarPQM) linked to genes encoding phenylpropanoid-degrading enzymes. The periplasmic solute-binding protein component of this transporter, TarP, has previously been shown to bind aromatic substrates. Here, we determine the high-resolution crystal structure of TarP from R. palustris as well as the structures of homologous proteins from the salt marsh bacterium Sagittula stellata and the halophile Chromohalobacter salexigens, which also grow on lignin-derived aromatics. In combination with tryptophan fluorescence ligand-binding assays, our ligand-bound co-crystal structures reveal the molecular basis for high-affinity recognition of phenylpropanoids by these TRAP transporters, which have potential for improving uptake of these compounds for biotechnological transformations of lignin.
The structural basis for high-affinity uptake of lignin-derived aromatic compounds by proteobacterial TRAP transporters.,Bisson C, Salmon RC, West L, Rafferty JB, Hitchcock A, Thomas GH, Kelly DJ FEBS J. 2021 Aug 10. doi: 10.1111/febs.16156. PMID:34375507[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bisson C, Salmon RC, West L, Rafferty JB, Hitchcock A, Thomas GH, Kelly DJ. The structural basis for high-affinity uptake of lignin-derived aromatic compounds by proteobacterial TRAP transporters. FEBS J. 2021 Aug 10. doi: 10.1111/febs.16156. PMID:34375507 doi:http://dx.doi.org/10.1111/febs.16156
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