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2O5P

Crystal structure of the full length ferric pyoverdine outer membrane receptor FpvA of Pseudomonas aeruginosa in its apo form

Summary for 2O5P
Entry DOI10.2210/pdb2o5p/pdb
Related1XKH 2iah
DescriptorFerripyoverdine receptor, PHOSPHATE ION, 3,6,9,12,15-PENTAOXATRICOSAN-1-OL (3 entities in total)
Functional Keywordsfpva, pyoverdine, pseudomonas, cobessi, transport protein
Biological sourcePseudomonas aeruginosa
Cellular locationCell outer membrane: P48632
Total number of polymer chains2
Total formula weight174412.37
Authors
Cobessi, D. (deposition date: 2006-12-06, release date: 2007-10-30, Last modification date: 2023-08-30)
Primary citationBrillet, K.,Journet, L.,Celia, H.,Paulus, L.,Stahl, A.,Pattus, F.,Cobessi, D.
A beta strand lock exchange for signal transduction in TonB-dependent transducers on the basis of a common structural motif.
Structure, 15:1383-1391, 2007
Cited by
PubMed Abstract: 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.
PubMed: 17997964
DOI: 10.1016/j.str.2007.08.013
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.77 Å)
Structure validation

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数据于2024-10-30公开中

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