1xkh
From Proteopedia
(New page: 200px<br /><applet load="1xkh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xkh, resolution 3.6Å" /> '''Pyoverdine outer memb...) |
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| - | [[Image:1xkh.gif|left|200px]]<br /><applet load="1xkh" size=" | + | [[Image:1xkh.gif|left|200px]]<br /><applet load="1xkh" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1xkh, resolution 3.6Å" /> | caption="1xkh, resolution 3.6Å" /> | ||
'''Pyoverdine outer membrane receptor FpvA from Pseudomonas aeruginosa PAO1 bound to pyoverdine'''<br /> | '''Pyoverdine outer membrane receptor FpvA from Pseudomonas aeruginosa PAO1 bound to pyoverdine'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The pyoverdine outer membrane receptor FpvA from Pseudomonas aeruginosa | + | The pyoverdine outer membrane receptor FpvA from Pseudomonas aeruginosa translocates ferric-pyoverdine across the outer membrane via an energy consuming mechanism that involves the inner membrane energy transducing complex of TonB-ExbB-ExbD and the proton motive force. We solved the crystal structure of FpvA loaded with iron-free pyoverdine at 3.6 angstroms resolution. The pyoverdine receptor is folded in two domains: a transmembrane 22-stranded beta-barrel domain occluded by an N-terminal domain containing a mixed four-stranded beta-sheet (the plug). The beta-strands of the barrel are connected by long extracellular loops and short periplasmic turns. The iron-free pyoverdine is bound at the surface of the receptor in a pocket lined with aromatic residues while the extracellular loops do not completely cover the pyoverdine binding site. The TonB box, which is involved in intermolecular contacts with the TonB protein of the inner membrane, is observed in an extended conformation. Comparison of this first reported structure of an iron-siderophore transporter from a bacterium other than Escherichia coli with the known structures of the E.coli TonB-dependent transporters reveals a high structural homology and suggests that a common sensing mechanism exists for the iron-loading status in all bacterial iron siderophore transporters. |
==About this Structure== | ==About this Structure== | ||
| - | 1XKH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] with SO4 and PVD as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1XKH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=PVD:'>PVD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XKH OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Pseudomonas aeruginosa]] | [[Category: Pseudomonas aeruginosa]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Abdallah, M | + | [[Category: Abdallah, M A.]] |
[[Category: Celia, H.]] | [[Category: Celia, H.]] | ||
[[Category: Cobessi, D.]] | [[Category: Cobessi, D.]] | ||
[[Category: Folschweiller, N.]] | [[Category: Folschweiller, N.]] | ||
[[Category: Pattus, F.]] | [[Category: Pattus, F.]] | ||
| - | [[Category: Schalk, I | + | [[Category: Schalk, I J.]] |
[[Category: PVD]] | [[Category: PVD]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: tonb dependent receptor]] | [[Category: tonb dependent receptor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:55:41 2008'' |
Revision as of 13:55, 21 February 2008
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Pyoverdine outer membrane receptor FpvA from Pseudomonas aeruginosa PAO1 bound to pyoverdine
Overview
The pyoverdine outer membrane receptor FpvA from Pseudomonas aeruginosa translocates ferric-pyoverdine across the outer membrane via an energy consuming mechanism that involves the inner membrane energy transducing complex of TonB-ExbB-ExbD and the proton motive force. We solved the crystal structure of FpvA loaded with iron-free pyoverdine at 3.6 angstroms resolution. The pyoverdine receptor is folded in two domains: a transmembrane 22-stranded beta-barrel domain occluded by an N-terminal domain containing a mixed four-stranded beta-sheet (the plug). The beta-strands of the barrel are connected by long extracellular loops and short periplasmic turns. The iron-free pyoverdine is bound at the surface of the receptor in a pocket lined with aromatic residues while the extracellular loops do not completely cover the pyoverdine binding site. The TonB box, which is involved in intermolecular contacts with the TonB protein of the inner membrane, is observed in an extended conformation. Comparison of this first reported structure of an iron-siderophore transporter from a bacterium other than Escherichia coli with the known structures of the E.coli TonB-dependent transporters reveals a high structural homology and suggests that a common sensing mechanism exists for the iron-loading status in all bacterial iron siderophore transporters.
About this Structure
1XKH is a Single protein structure of sequence from Pseudomonas aeruginosa with and as ligands. Full crystallographic information is available from OCA.
Reference
The crystal structure of the pyoverdine outer membrane receptor FpvA from Pseudomonas aeruginosa at 3.6 angstroms resolution., Cobessi D, Celia H, Folschweiller N, Schalk IJ, Abdallah MA, Pattus F, J Mol Biol. 2005 Mar 18;347(1):121-34. Epub 2005 Jan 21. PMID:15733922
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