3qlb: Difference between revisions

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[[Image:3qlb.jpg|left|200px]]


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==Enantiopyochelin outer membrane TonB-dependent transporter from Pseudomonas fluorescens bound to the ferri-enantiopyochelin==
The line below this paragraph, containing "STRUCTURE_3qlb", creates the "Structure Box" on the page.
<StructureSection load='3qlb' size='340' side='right'caption='[[3qlb]], [[Resolution|resolution]] 3.26&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[3qlb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_fluorescens Pseudomonas fluorescens]. 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>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.26&#8491;</td></tr>
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<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>
{{STRUCTURE_3qlb|  PDB=3qlb  |  SCENE=  }}
<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>
== Function ==
[https://www.uniprot.org/uniprot/C5I2D9_PSEFL C5I2D9_PSEFL]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Pyochelin (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.


===Enantiopyochelin outer membrane TonB-dependent transporter from Pseudomonas fluorescens bound to the ferri-enantiopyochelin===
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<ref>PMID:21902256</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
The line below this paragraph, {{ABSTRACT_PUBMED_21902256}}, adds the Publication Abstract to the page
<div class="pdbe-citations 3qlb" style="background-color:#fffaf0;"></div>
(as it appears on PubMed at http://www.pubmed.gov), where 21902256 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_21902256}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
[[3qlb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_fluorescens Pseudomonas fluorescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QLB OCA].
 
==Reference==
<ref group="xtra">PMID:021902256</ref><references group="xtra"/>
[[Category: Pseudomonas fluorescens]]
[[Category: Pseudomonas fluorescens]]
[[Category: Brillet, K.]]
[[Category: Brillet K]]
[[Category: Cobessi, D.]]
[[Category: Cobessi D]]
[[Category: Mislin, G L.A.]]
[[Category: Mislin GLA]]
[[Category: Noel, S.]]
[[Category: Noel S]]
[[Category: Reimmann, C.]]
[[Category: Reimmann C]]
[[Category: Schalk, I J.]]
[[Category: Schalk IJ]]
[[Category: Ferri-enantiopyochelin]]
[[Category: Membrane protein]]
[[Category: Metal transport]]
[[Category: Outer membrane]]
[[Category: Transport]]

Latest revision as of 20:14, 1 November 2023

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

3qlb is a 2 chain structure with sequence from Pseudomonas fluorescens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.26Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

C5I2D9_PSEFL

Publication Abstract from PubMed

Pyochelin (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

  1. ↑ Brillet K, Reimmann C, Mislin GL, Noel S, Rognan D, Schalk IJ, Cobessi D. Pyochelin enantiomers and their outer-membrane siderophore transporters in fluorescent pseudomonads: structural bases for unique enantiospecific recognition. J Am Chem Soc. 2011 Oct 19;133(41):16503-9. Epub 2011 Sep 23. PMID:21902256 doi:10.1021/ja205504z

3qlb, resolution 3.26Å

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