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< | ==Structures of P. aeruginosa FpvA bound to heterologous pyoverdines: FpvA-Pvd(DSM50106)-Fe complex== | ||
<StructureSection load='2w6t' size='340' side='right'caption='[[2w6t]], [[Resolution|resolution]] 2.90Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2w6t]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1] and [https://en.wikipedia.org/wiki/Pseudomonas_fluorescens Pseudomonas fluorescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W6T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2W6T FirstGlance]. <br> | |||
or | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</td></tr> | ||
-- | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DSN:D-SERINE'>DSN</scene>, <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=ORN:L-ORNITHINE'>ORN</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=PRD_000728:Synthetic+PYOVERDINE+Fe+Complex'>PRD_000728</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2w6t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w6t OCA], [https://pdbe.org/2w6t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2w6t RCSB], [https://www.ebi.ac.uk/pdbsum/2w6t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2w6t ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/FPVA_PSEAE FPVA_PSEAE] Receptor for the siderophore ferripyoverdine. | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w6/2w6t_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2w6t ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:19504741</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2w6t" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
*[[Ferripyoverdine receptor|Ferripyoverdine receptor]] | |||
[[Category: Pseudomonas | == References == | ||
[[Category: Celia | <references/> | ||
[[Category: Greenwald | __TOC__ | ||
[[Category: Gruffaz | </StructureSection> | ||
[[Category: Meyer | [[Category: Large Structures]] | ||
[[Category: Nader | [[Category: Pseudomonas aeruginosa PAO1]] | ||
[[Category: Pattus | [[Category: Pseudomonas fluorescens]] | ||
[[Category: Schalk | [[Category: Celia H]] | ||
[[Category: Greenwald J]] | |||
[[Category: Gruffaz C]] | |||
[[Category: Meyer J-M]] | |||
[[Category: Nader M]] | |||
[[Category: Pattus F]] | |||
[[Category: Schalk IJ]] | |||
Latest revision as of 18:45, 13 December 2023
Structures of P. aeruginosa FpvA bound to heterologous pyoverdines: FpvA-Pvd(DSM50106)-Fe complexStructures of P. aeruginosa FpvA bound to heterologous pyoverdines: FpvA-Pvd(DSM50106)-Fe complex
Structural highlights
FunctionFPVA_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 PubMedThe 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 AlsoReferences |
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