6H7V

Crystal structure of BauA, the Ferric preacinetobactin receptor from Acinetobacter baumannii

Summary for 6H7V

• Entry DOI: 10.2210/pdb6h7v/pdb
• Related: 6H7F
• Descriptor: Ligand-gated channel protein, 1,2-ETHANEDIOL, (HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE, ... (4 entities in total)
• Functional Keywords: baua, outer-membrane transporter, membrane protein
• Biological source: Acinetobacter baumannii (strain ATCC 19606 / DSM 30007 / CIP 70.34 / JCM 6841 / NBRC 109757 / NCIMB 12457 / NCTC 12156 / 81)
• Total number of polymer chains: 3
• Total formula weight: 235161.29

Authors

Moynie, L.,Naismith, J.H. (deposition date: 2018-07-31, release date: 2018-10-10, Last modification date: 2024-10-23)

Primary citation

Moynie, L.,Serra, I.,Scorciapino, M.A.,Oueis, E.,Page, M.G.,Ceccarelli, M.,Naismith, J.H.
Preacinetobactin not acinetobactin is essential for iron uptake by the BauA transporter of the pathogenAcinetobacter baumannii.
Elife, 7:-, 2018

PubMed Abstract: New strategies are urgently required to develop antibiotics. The siderophore uptake system has attracted considerable attention, but rational design of siderophore antibiotic conjugates requires knowledge of recognition by the cognate outer-membrane transporter. is a serious pathogen, which utilizes (pre)acinetobactin to scavenge iron from the host. We report the structure of the (pre)acinetobactin transporter BauA bound to the siderophore, identifying the structural determinants of recognition. Detailed biophysical analysis confirms that BauA recognises preacinetobactin. We show that acinetobactin is not recognised by the protein, thus preacinetobactin is essential for iron uptake. The structure shows and NMR confirms that under physiological conditions, a molecule of acinetobactin will bind to two free coordination sites on the iron preacinetobactin complex. The ability to recognise a heterotrimeric iron-preacinetobactin-acinetobactin complex may rationalize contradictory reports in the literature. These results open new avenues for the design of novel antibiotic conjugates (trojan horse) antibiotics.

PubMed: 30558715
DOI: 10.7554/eLife.42270

Experimental method

X-RAY DIFFRACTION (2.54 Å)