2o5p | pdb_00002o5p
Crystal structure of the full length ferric pyoverdine outer membrane receptor FpvA of Pseudomonas aeruginosa in its apo form
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| 2o5p, resolution 2.77Å | |||||||||||||
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| Ligands: | N8E, PO4 | ||||||||||||
| Gene: | fpvA (Pseudomonas aeruginosa) | ||||||||||||
| Related: | 1XKH, 2iah
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Overview
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.
About this Structure
2O5P is a Single protein structure of sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.
Reference
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
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