Imperial College London

DrKonstantinosBeis

Faculty of Natural SciencesDepartment 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{Ghilarov:2021:10.1126/sciadv.abj5363,
author = {Ghilarov, D and Inaba-Inoue, S and Stepien, P and Qu, F and Michalczyk, E and Pakosz, Z and Nomura, N and Ogasawara, S and Walker, GC and Rebuffat, S and Iwata, S and Heddle, JG and Beis, K},
doi = {10.1126/sciadv.abj5363},
journal = {Science Advances},
pages = {1--10},
title = {Molecular mechanism of SbmA, a promiscuous transporter exploited by antimicrobial peptides},
url = {http://dx.doi.org/10.1126/sciadv.abj5363},
volume = {7},
year = {2021}
}

RIS format (EndNote, RefMan)

TY  - JOUR
AB - Antibiotic metabolites and antimicrobial peptides mediate competition between bacterial species. Many of them hijack inner and outer membrane proteins to enter cells. Sensitivity of enteric bacteria to multiple peptide antibiotics is controlled by the single inner membrane protein SbmA. To establish the molecular mechanism of peptide transport by SbmA and related BacA, we determined their cryo–electron microscopy structures at 3.2 and 6 Å local resolution, respectively. The structures show a previously unknown fold, defining a new class of secondary transporters named SbmA-like peptide transporters. The core domain includes conserved glutamates, which provide a pathway for proton translocation, powering transport. The structures show an outward-open conformation with a large cavity that can accommodate diverse substrates. We propose a molecular mechanism for antibacterial peptide uptake paving the way for creation of narrow-targeted therapeutics.
AU - Ghilarov,D
AU - Inaba-Inoue,S
AU - Stepien,P
AU - Qu,F
AU - Michalczyk,E
AU - Pakosz,Z
AU - Nomura,N
AU - Ogasawara,S
AU - Walker,GC
AU - Rebuffat,S
AU - Iwata,S
AU - Heddle,JG
AU - Beis,K
DO - 10.1126/sciadv.abj5363
EP - 10
PY - 2021///
SN - 2375-2548
SP - 1
TI - Molecular mechanism of SbmA, a promiscuous transporter exploited by antimicrobial peptides
T2 - Science Advances
UR - http://dx.doi.org/10.1126/sciadv.abj5363
UR - https://www.science.org/doi/10.1126/sciadv.abj5363
UR - http://hdl.handle.net/10044/1/91606
VL - 7
ER -