6Z2N
Crystal structure of the ferric enterobactin receptor (PfeA) in complex with BCV-L6
This is a non-PDB format compatible entry.
Summary for 6Z2N
Entry DOI | 10.2210/pdb6z2n/pdb |
Descriptor | Ferric enterobactin receptor, 1,2-ETHANEDIOL, BCV-L6, ... (4 entities in total) |
Functional Keywords | tonb dependent transporter, siderophore, membrane protein |
Biological source | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
Total number of polymer chains | 1 |
Total formula weight | 79753.24 |
Authors | Naismith, J.H.,Moynie, L.M. (deposition date: 2020-05-18, release date: 2021-01-20, Last modification date: 2024-11-13) |
Primary citation | Moynie, L.,Hoegy, F.,Milenkovic, S.,Munier, M.,Paulen, A.,Gasser, V.,Faucon, A.L.,Zill, N.,Naismith, J.H.,Ceccarelli, M.,Schalk, I.J.,Mislin, G.L.A. Hijacking of the Enterobactin Pathway by a Synthetic Catechol Vector Designed for Oxazolidinone Antibiotic Delivery in Pseudomonas aeruginosa. Acs Infect Dis., 2022 Cited by PubMed Abstract: Enterobactin (ENT) is a tris-catechol siderophore used to acquire iron by multiple bacterial species. These ENT-dependent iron uptake systems have often been considered as potential gates in the bacterial envelope through which one can shuttle antibiotics (Trojan horse strategy). In practice, siderophore analogues containing catechol moieties have shown promise as vectors to which antibiotics may be attached. Bis- and tris-catechol vectors (BCVs and TCVs, respectively) were shown using structural biology and molecular modeling to mimic ENT binding to the outer membrane transporter PfeA in . TCV but not BCV appears to cross the outer membrane via PfeA when linked to an antibiotic (linezolid). TCV is therefore a promising vector for Trojan horse strategies against , confirming the ENT-dependent iron uptake system as a gate to transport antibiotics into cells. PubMed: 35881068DOI: 10.1021/acsinfecdis.2c00202 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.029 Å) |
Structure validation
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