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| ==Crystal structure of the full length ferric pyoverdine outer membrane receptor FpvA of Pseudomonas aeruginosa in its apo form== | | ==Crystal structure of the full length ferric pyoverdine outer membrane receptor FpvA of Pseudomonas aeruginosa in its apo form== |
- | <StructureSection load='2o5p' size='340' side='right' caption='[[2o5p]], [[Resolution|resolution]] 2.77Å' scene=''> | + | <StructureSection load='2o5p' size='340' side='right'caption='[[2o5p]], [[Resolution|resolution]] 2.77Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[2o5p]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O5P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2O5P FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2o5p]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O5P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O5P FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=N8E:3,6,9,12,15-PENTAOXATRICOSAN-1-OL'>N8E</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 2.77Å</td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1xkh|1xkh]], [[2iah|2iah]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=N8E:3,6,9,12,15-PENTAOXATRICOSAN-1-OL'>N8E</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fpvA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</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=2o5p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o5p OCA], [https://pdbe.org/2o5p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o5p RCSB], [https://www.ebi.ac.uk/pdbsum/2o5p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o5p ProSAT]</span></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=2o5p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o5p OCA], [http://pdbe.org/2o5p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2o5p RCSB], [http://www.ebi.ac.uk/pdbsum/2o5p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2o5p ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://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]] |
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Cobessi, D]] | + | [[Category: Large Structures]] |
- | [[Category: Cobessi]] | + | [[Category: Pseudomonas aeruginosa]] |
- | [[Category: Fpva]] | + | [[Category: Cobessi D]] |
- | [[Category: Pseudomona]]
| + | |
- | [[Category: Pyoverdine]]
| + | |
- | [[Category: Transport protein]]
| + | |
| Structural highlights
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
Transport of molecules larger than 600 Da across the outer membrane involves TonB-dependent receptors and TonB-ExbB-ExbD of the inner membrane. The transport is energy consuming, and involves direct interactions between a short N-terminal sequence of receptor, called the TonB box, and TonB. We solved the structure of the ferric pyoverdine (Pvd-Fe) outer membrane receptor FpvA from Pseudomonas aeruginosa in its apo form. Structure analyses show that residues of the TonB box are in a beta strand which interacts through a mixed four-stranded beta sheet with the periplasmic signaling domain involved in interactions with an inner membrane sigma regulator. In this conformation, the TonB box cannot form a four-stranded beta sheet with TonB. The FhuA-TonB or BtuB-TonB structures show that the TonB-FpvA interactions require a conformational change which involves a beta strand lock-exchange mechanism. This mechanism is compatible with movements of the periplasmic domain deduced from crystallographic analyses of FpvA, FpvA-Pvd, and FpvA-Pvd-Fe.
A beta strand lock exchange for signal transduction in TonB-dependent transducers on the basis of a common structural motif.,Brillet K, Journet L, Celia H, Paulus L, Stahl A, Pattus F, Cobessi D Structure. 2007 Nov;15(11):1383-91. PMID:17997964[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Brillet K, Journet L, Celia H, Paulus L, Stahl A, Pattus F, Cobessi D. A beta strand lock exchange for signal transduction in TonB-dependent transducers on the basis of a common structural motif. Structure. 2007 Nov;15(11):1383-91. PMID:17997964 doi:10.1016/j.str.2007.08.013
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