3qlb: Difference between revisions
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==Enantiopyochelin outer membrane TonB-dependent transporter from Pseudomonas fluorescens bound to the ferri-enantiopyochelin== | ==Enantiopyochelin outer membrane TonB-dependent transporter from Pseudomonas fluorescens bound to the ferri-enantiopyochelin== | ||
<StructureSection load='3qlb' size='340' side='right' caption='[[3qlb]], [[Resolution|resolution]] 3.26Å' scene=''> | <StructureSection load='3qlb' size='340' side='right'caption='[[3qlb]], [[Resolution|resolution]] 3.26Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3qlb]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3qlb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_fluorescens_liquefaciens"_flugge_1886 "bacillus fluorescens liquefaciens" flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QLB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QLB FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=EFE:ENANTIO-PYOCHELIN+FE(III)'>EFE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=EFE:ENANTIO-PYOCHELIN+FE(III)'>EFE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fetA ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fetA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=294 "Bacillus fluorescens liquefaciens" Flugge 1886])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3qlb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qlb OCA], [https://pdbe.org/3qlb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qlb RCSB], [https://www.ebi.ac.uk/pdbsum/3qlb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qlb ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
| Line 22: | Line 22: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bacillus fluorescens liquefaciens flugge 1886]] | [[Category: Bacillus fluorescens liquefaciens flugge 1886]] | ||
[[Category: Large Structures]] | |||
[[Category: Brillet, K]] | [[Category: Brillet, K]] | ||
[[Category: Cobessi, D]] | [[Category: Cobessi, D]] | ||
Revision as of 09:13, 8 June 2022
Enantiopyochelin outer membrane TonB-dependent transporter from Pseudomonas fluorescens bound to the ferri-enantiopyochelinEnantiopyochelin outer membrane TonB-dependent transporter from Pseudomonas fluorescens bound to the ferri-enantiopyochelin
Structural highlights
Publication Abstract from PubMedPyochelin (Pch) and enantiopyochelin (EPch) are enantiomeric siderophores, with three chiral centers, produced under iron limitation conditions by Pseudomonas aeruginosa and Pseudomonas fluorescens , respectively. After iron chelation in the extracellular medium, Pch-Fe and EPch-Fe are recognized and transported by their specific outer-membrane transporters: FptA in P. aeruginosa and FetA in P. fluorescens . Structural analysis of FetA-EPch-Fe and FptA-Pch-Fe, combined with mutagenesis and docking studies revealed the structural basis of the stereospecific recognition of these enantiomers by their respective transporters. Whereas FetA and FptA have a low sequence identity but high structural homology, the Pch and EPch binding pockets do not share any structural homology, but display similar physicochemical properties. The stereospecific recognition of both enantiomers by their corresponding transporters is imposed by the configuration of the siderophore's C4 and C2 chiral centers. This recognition involves specific hydrogen bonds between the Arg91 guanidinium group and EPch-Fe for FetA and between the Leu117-Leu116 main chain and Pch-Fe for FptA. FetA and FptA are the first membrane receptors to be structurally described with opposite binding enantioselectivities for their ligands, giving insights into the structural basis of their enantiospecificity. Pyochelin enantiomers and their outer-membrane siderophore transporters in fluorescent pseudomonads: structural bases for unique enantiospecific recognition.,Brillet K, Reimmann C, Mislin GL, Noel S, Rognan D, Schalk IJ, Cobessi D J Am Chem Soc. 2011 Oct 19;133(41):16503-9. Epub 2011 Sep 23. PMID:21902256[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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