The crystal structure of the pyoverdine outer membrane receptor FpvA from Pseudomonas aeruginosa at 3.6 angstroms resolution
| Autor: | Isabelle J. Schalk, Nicolas Folschweiller, Franc Pattus, David Cobessi, Mohamed A. Abdallah, Hervé Celia |
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| Přispěvatelé: | Institut Gilbert-Laustriat : Biomolécules, Biotechnologie, Innovation Thérapeutique, Université Louis Pasteur - Strasbourg I-Centre National de la Recherche Scientifique (CNRS), Klotz, Evelyne |
| Jazyk: | angličtina |
| Rok vydání: | 2005 |
| Předmět: |
Models
Molecular Protein Folding Secondary MESH: Protein Structure Quaternary MESH: Protein Structure Secondary Siderophores MESH: Amino Acid Sequence Crystallography X-Ray Protein Structure Secondary chemistry.chemical_compound Protein structure Structural Biology Models Non-U.S. Gov't Oligopeptides/chemistry/metabolism 0303 health sciences Pyoverdine Crystallography Siderophores/*chemistry/metabolism Transmembrane protein [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biomolecules [q-bio.BM] Protein folding Bacterial outer membrane Oligopeptides MESH: Models Molecular Bacterial Outer Membrane Proteins Protein Structure MESH: Protein Folding Molecular Sequence Data Biology Bacterial Outer Membrane Proteins/*chemistry/metabolism Research Support Quaternary 03 medical and health sciences Allosteric Regulation Inner membrane Amino Acid Sequence MESH: Siderophores Protein Structure Quaternary Molecular Biology 030304 developmental biology MESH: Molecular Sequence Data Binding Sites 030306 microbiology MESH: Bacterial Outer Membrane Proteins Molecular Periplasmic space MESH: Crystallography X-Ray chemistry Membrane protein MESH: Binding Sites Biophysics X-Ray |
| Zdroj: | Journal of Molecular Biology Journal of Molecular Biology, Elsevier, 2005, 347, pp.121-34 Journal of Molecular Biology, Elsevier, 2005, 347 (1), pp.121-34. ⟨10.1016/j.jmb.2005.01.021⟩ |
| ISSN: | 0022-2836 1089-8638 |
| DOI: | 10.1016/j.jmb.2005.01.021⟩ |
| Popis: | 0022-2836 (Print) Journal Article; 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. |
| Databáze: | OpenAIRE |
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