Imperial College London
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DrKonstantinosBeis

Faculty of Natural Sciences, Department of Life Sciences

Reader in Membrane Protein Structural Biology
 
 
 
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Contact

 

konstantinos.beis Website

 
 
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Location

 

1-12Diamond Light Source LtdHarwell Science and Innovation Campus

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Summary

 

Publications

Citation

BibTex format

@article{Bountra:2017:10.15252/embj.201797278,
author = {Bountra, K and Hagelueken, G and Choudhury, HG and Corradi, V and El, Omari K and Wagner, A and Mathavan, I and Zirah, S and Yuan, Wahlgren W and Tieleman, DP and Schiemann, O and Rebuffat, S and Beis, K},
doi = {10.15252/embj.201797278},
journal = {The EMBO Journal},
pages = {3062--3079},
title = {Structural basis for antibacterial peptide self-immunity by the bacterial ABC transporter McjD},
url = {http://dx.doi.org/10.15252/embj.201797278},
volume = {36},
year = {2017}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - Certain pathogenic bacteria produce and release toxic peptides to ensure either nutrient availability or evasion from the immune system. These peptides are also toxic to the producing bacteria that utilize dedicated ABC transporters to provide selfimmunity. The ABC transporter McjD exports the antibacterial peptide MccJ25 in Escherichia coli. Our previously determined McjD structure provided some mechanistic insights into antibacterial peptide efflux. In this study, we have determined its structure in a novel conformation, apo inwardoccluded and a new nucleotidebound state, highenergy outwardoccluded intermediate state, with a defined ligand binding cavity. Predictive cysteine crosslinking in E. coli membranes and PELDOR measurements along the transport cycle indicate that McjD does not undergo major conformational changes as previously proposed for multidrug ABC exporters. Combined with transport assays and molecular dynamics simulations, we propose a novel mechanism for toxic peptide ABC exporters that only requires the transient opening of the cavity for release of the peptide. We propose that shielding of the cavity ensures that the transporter is available to export the newly synthesized peptides, preventing toxiclevel buildup.
AU  - Bountra,K
AU  - Hagelueken,G
AU  - Choudhury,HG
AU  - Corradi,V
AU  - El,Omari K
AU  - Wagner,A
AU  - Mathavan,I
AU  - Zirah,S
AU  - Yuan,Wahlgren W
AU  - Tieleman,DP
AU  - Schiemann,O
AU  - Rebuffat,S
AU  - Beis,K
DO  - 10.15252/embj.201797278
EP  - 3079
PY  - 2017///
SN  - 0261-4189
SP  - 3062
TI  - Structural basis for antibacterial peptide self-immunity by the bacterial ABC transporter McjD
T2  - The EMBO Journal
UR  - http://dx.doi.org/10.15252/embj.201797278
UR  - https://www.embopress.org/doi/epdf/10.15252/embj.201797278
UR  - http://hdl.handle.net/10044/1/50390
VL  - 36
ER  -
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