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| | ==Structure of the FpvAI-pyocin S2 complex== | | ==Structure of the FpvAI-pyocin S2 complex== |
| - | <StructureSection load='5odw' size='340' side='right' caption='[[5odw]], [[Resolution|resolution]] 2.80Å' scene=''> | + | <StructureSection load='5odw' size='340' side='right'caption='[[5odw]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5odw]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseae Pseae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ODW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ODW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5odw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ODW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ODW FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.8Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fpvA, PA2398 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=208964 PSEAE]), pys2, PA1150 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=208964 PSEAE])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=5odw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5odw OCA], [http://pdbe.org/5odw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5odw RCSB], [http://www.ebi.ac.uk/pdbsum/5odw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5odw 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=5odw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5odw OCA], [https://pdbe.org/5odw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5odw RCSB], [https://www.ebi.ac.uk/pdbsum/5odw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5odw ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/FPVA_PSEAE FPVA_PSEAE]] Receptor for the siderophore ferripyoverdine. [[http://www.uniprot.org/uniprot/PYS2_PSEAE PYS2_PSEAE]] Causes breakdown of chromosomal DNA as well as complete inhibition of lipid synthesis in sensitive cells. | + | [https://www.uniprot.org/uniprot/FPVA_PSEAE FPVA_PSEAE] Receptor for the siderophore ferripyoverdine. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5odw" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5odw" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Ferripyoverdine receptor|Ferripyoverdine receptor]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Pseae]] | + | [[Category: Large Structures]] |
| - | [[Category: Joshi, A]] | + | [[Category: Pseudomonas aeruginosa PAO1]] |
| - | [[Category: Kleanthous, C]] | + | [[Category: Joshi A]] |
| - | [[Category: White, P]] | + | [[Category: Kleanthous C]] |
| - | [[Category: Antimicrobial protein]] | + | [[Category: White P]] |
| - | [[Category: Membrane protein complex]]
| + | |
| - | [[Category: Protein transport]]
| + | |
| Structural highlights
Function
FPVA_PSEAE Receptor for the siderophore ferripyoverdine.
Publication Abstract from PubMed
Unlike their descendants, mitochondria and plastids, bacteria do not have dedicated protein import systems. However, paradoxically, import of protein bacteriocins, the mechanisms of which are poorly understood, underpins competition among pathogenic and commensal bacteria alike. Here, using X-ray crystallography, isothermal titration calorimetry, confocal fluorescence microscopy, and in vivo photoactivatable cross-linking of stalled translocation intermediates, we demonstrate how the iron transporter FpvAI in the opportunistic pathogen Pseudomonas aeruginosa is hijacked to translocate the bacteriocin pyocin S2 (pyoS2) across the outer membrane (OM). FpvAI is a TonB-dependent transporter (TBDT) that actively imports the small siderophore ferripyoverdine (Fe-Pvd) by coupling to the proton motive force (PMF) via the inner membrane (IM) protein TonB1. The crystal structure of the N-terminal domain of pyoS2 (pyoS2NTD) bound to FpvAI (Kd = 240 pM) reveals that the pyocin mimics Fe-Pvd, inducing the same conformational changes in the receptor. Mimicry leads to fluorescently labeled pyoS2NTD being imported into FpvAI-expressing P. aeruginosa cells by a process analogous to that used by bona fide TBDT ligands. PyoS2NTD induces unfolding by TonB1 of a force-labile portion of the plug domain that normally occludes the central channel of FpvAI. The pyocin is then dragged through this narrow channel following delivery of its own TonB1-binding epitope to the periplasm. Hence, energized nutrient transporters in bacteria also serve as rudimentary protein import systems, which, in the case of FpvAI, results in a protein antibiotic 60-fold bigger than the transporter's natural substrate being translocated across the OM.
Exploitation of an iron transporter for bacterial protein antibiotic import.,White P, Joshi A, Rassam P, Housden NG, Kaminska R, Goult JD, Redfield C, McCaughey LC, Walker D, Mohammed S, Kleanthous C Proc Natl Acad Sci U S A. 2017 Oct 25. pii: 201713741. doi:, 10.1073/pnas.1713741114. PMID:29078392[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ White P, Joshi A, Rassam P, Housden NG, Kaminska R, Goult JD, Redfield C, McCaughey LC, Walker D, Mohammed S, Kleanthous C. Exploitation of an iron transporter for bacterial protein antibiotic import. Proc Natl Acad Sci U S A. 2017 Oct 25. pii: 201713741. doi:, 10.1073/pnas.1713741114. PMID:29078392 doi:http://dx.doi.org/10.1073/pnas.1713741114
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