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| {{STRUCTURE_2o5p| PDB=2o5p | SCENE= }} | | {{STRUCTURE_2o5p| PDB=2o5p | SCENE= }} |
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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=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17997964}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17997964 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17997964}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Pyoverdine]] | | [[Category: Pyoverdine]] |
| [[Category: Transport protein]] | | [[Category: Transport protein]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 10:21:40 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:35:13 2008'' |
