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| | <StructureSection load='2w78' size='340' side='right'caption='[[2w78]], [[Resolution|resolution]] 3.00Å' scene=''> | | <StructureSection load='2w78' size='340' side='right'caption='[[2w78]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2w78]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseae Pseae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W78 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2W78 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2w78]] is a 3 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=2W78 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2W78 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=N8E:3,6,9,12,15-PENTAOXATRICOSAN-1-OL'>N8E</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=PVE:(1S)-1-CARBOXY-5-[(3-CARBOXYPROPANOYL)AMINO]-8,9-DIHYDROXY-1,2,3,4-TETRAHYDROPYRIMIDO[1,2-A]QUINOLIN-11-IUM'>PVE</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]] 3Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=FH7:N^5^-FORMYL-N^5^-HYDROXY-D-ORNITHINE'>FH7</scene>, <scene name='pdbligand=FHO:N^5^-FORMYL-N^5^-HYDROXY-L-ORNITHINE'>FHO</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=FH7:N^5^-FORMYL-N^5^-HYDROXY-D-ORNITHINE'>FH7</scene>, <scene name='pdbligand=FHO:N^5^-FORMYL-N^5^-HYDROXY-L-ORNITHINE'>FHO</scene>, <scene name='pdbligand=N8E:3,6,9,12,15-PENTAOXATRICOSAN-1-OL'>N8E</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=PVE:(1S)-1-CARBOXY-5-[(3-CARBOXYPROPANOYL)AMINO]-8,9-DIHYDROXY-1,2,3,4-TETRAHYDROPYRIMIDO[1,2-A]QUINOLIN-11-IUM'>PVE</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;'>[[1xkh|1xkh]], [[2w16|2w16]], [[2w6t|2w6t]], [[2w6u|2w6u]], [[2w75|2w75]], [[2w76|2w76]], [[2w77|2w77]]</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=2w78 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w78 OCA], [https://pdbe.org/2w78 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2w78 RCSB], [https://www.ebi.ac.uk/pdbsum/2w78 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2w78 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=2w78 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w78 OCA], [https://pdbe.org/2w78 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2w78 RCSB], [https://www.ebi.ac.uk/pdbsum/2w78 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2w78 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/FPVA_PSEAE FPVA_PSEAE]] Receptor for the siderophore ferripyoverdine.
| + | [https://www.uniprot.org/uniprot/FPVA_PSEAE FPVA_PSEAE] Receptor for the siderophore ferripyoverdine. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 38: |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pseae]] | + | [[Category: Pseudomonas aeruginosa PAO1]] |
| - | [[Category: Celia, H]] | + | [[Category: Celia H]] |
| - | [[Category: Greenwald, J]] | + | [[Category: Greenwald J]] |
| - | [[Category: Gruffaz, C]] | + | [[Category: Gruffaz C]] |
| - | [[Category: Meyer, J M]] | + | [[Category: Meyer J-M]] |
| - | [[Category: Nader, M]] | + | [[Category: Nader M]] |
| - | [[Category: Pattus, F]] | + | [[Category: Pattus F]] |
| - | [[Category: Schalk, I J]] | + | [[Category: Schalk IJ]] |
| - | [[Category: Cell membrane]]
| + | |
| - | [[Category: Cell outer membrane]]
| + | |
| - | [[Category: Fpva]]
| + | |
| - | [[Category: Ion transport]]
| + | |
| - | [[Category: Iron]]
| + | |
| - | [[Category: Iron transport]]
| + | |
| - | [[Category: Membrane]]
| + | |
| - | [[Category: Receptor]]
| + | |
| - | [[Category: Siderophore]]
| + | |
| - | [[Category: Tonb box]]
| + | |
| - | [[Category: Tonb-dependent transporter]]
| + | |
| - | [[Category: Transport]]
| + | |
| Structural highlights
2w78 is a 3 chain structure with sequence from Pseudomonas aeruginosa PAO1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 3Å |
| Ligands: | , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
FPVA_PSEAE Receptor for the siderophore ferripyoverdine.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The first step in the specific uptake of iron via siderophores in Gram-negative bacteria is the recognition and binding of a ferric siderophore by its cognate receptor. We investigated the molecular basis of this event through structural and biochemical approaches. FpvA, the pyoverdine-Fe transporter from Pseudomonas aeruginosa ATCC 15692 (PAO1 strain), is able to transport ferric-pyoverdines originating from other species, whereas most fluorescent pseudomonads are only able to use the one they produce among the more than 100 known different pyoverdines. We solved the structure of FpvA bound to non-cognate pyoverdines of high- or low-affinity and found a close correlation between receptor-ligand structure and the measured affinities. The structure of the first amino acid residues of the pyoverdine chain distinguished the high- and low-affinity binders while the C-terminal portion of the pyoverdines, often cyclic, does not appear to contribute extensively to the interaction between the siderophore and its transporter. The specificity of the ferric-pyoverdine binding site of FpvA is conferred by the structural elements common to all ferric-pyoverdines, i.e. the chromophore, iron, and its chelating groups.
FpvA bound to non-cognate pyoverdines: molecular basis of siderophore recognition by an iron transporter.,Greenwald J, Nader M, Celia H, Gruffaz C, Geoffroy V, Meyer JM, Schalk IJ, Pattus F Mol Microbiol. 2009 Jun;72(5):1246-59. PMID:19504741[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Greenwald J, Nader M, Celia H, Gruffaz C, Geoffroy V, Meyer JM, Schalk IJ, Pattus F. FpvA bound to non-cognate pyoverdines: molecular basis of siderophore recognition by an iron transporter. Mol Microbiol. 2009 Jun;72(5):1246-59. PMID:19504741
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