1xkh
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(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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Revision as of 04:00, 21 November 2007
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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 SO4 and PVD 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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