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| | <StructureSection load='3qk6' size='340' side='right'caption='[[3qk6]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='3qk6' size='340' side='right'caption='[[3qk6]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3qk6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecout Ecout]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QK6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QK6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3qk6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_UTI89 Escherichia coli UTI89]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QK6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QK6 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=UNL:UNKNOWN+LIGAND'>UNL</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]] 2.4Å</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=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;'>[[3p7i|3p7i]]</div></td></tr>
| + | |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">phnD, UTI89_C4699 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=364106 ECOUT])</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=3qk6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qk6 OCA], [https://pdbe.org/3qk6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qk6 RCSB], [https://www.ebi.ac.uk/pdbsum/3qk6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qk6 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=3qk6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qk6 OCA], [https://pdbe.org/3qk6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qk6 RCSB], [https://www.ebi.ac.uk/pdbsum/3qk6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qk6 ProSAT]</span></td></tr> |
| | </table> | | </table> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecout]] | + | [[Category: Escherichia coli UTI89]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Alicea, I]] | + | [[Category: Alicea I]] |
| - | [[Category: Schreiter, E R]] | + | [[Category: Schreiter ER]] |
| - | [[Category: Phosphonate transport protein]]
| + | |
| - | [[Category: Transport protein]]
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| Structural highlights
Publication Abstract from PubMed
The phnD gene of Escherichia coli encodes the periplasmic binding protein of the phosphonate (Pn) uptake and utilization pathway. We have crystallized and determined structures of E. coli PhnD (EcPhnD) in the absence of ligand and in complex with the environmentally abundant 2-aminoethylphosphonate (2AEP). Similar to other bacterial periplasmic binding proteins, 2AEP binds near the center of mass of EcPhnD in a cleft formed between two lobes. Comparison of the open, unliganded structure with the closed 2AEP-bound structure shows that the two lobes pivot around a hinge by approximately 70 degrees between the two states. Extensive hydrogen bonding and electrostatic interactions stabilize 2AEP, which binds to EcPhnD with low nanomolar affinity. These structures provide insight into Pn uptake by bacteria and facilitated the rational design of high signal-to-noise Pn biosensors based on both coupled small-molecule dyes and autocatalytic fluorescent proteins.
Structure of the Escherichia coli Phosphonate Binding Protein PhnD and Rationally Optimized Phosphonate Biosensors.,Alicea I, Marvin JS, Miklos AE, Ellington AD, Looger LL, Schreiter ER J Mol Biol. 2011 Dec 2;414(3):356-69. Epub 2011 Oct 12. PMID:22019591[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Alicea I, Marvin JS, Miklos AE, Ellington AD, Looger LL, Schreiter ER. Structure of the Escherichia coli Phosphonate Binding Protein PhnD and Rationally Optimized Phosphonate Biosensors. J Mol Biol. 2011 Dec 2;414(3):356-69. Epub 2011 Oct 12. PMID:22019591 doi:10.1016/j.jmb.2011.09.047
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