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MOMP from Campylobacter jejuni is a trimer of 18-stranded β–barrel monomers with a Ca2+ ion bound at the constriction zone

Research output: Contribution to journalArticlepeer-review

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MOMP from Campylobacter jejuni is a trimer of 18-stranded β–barrel monomers with a Ca2+ ion bound at the constriction zone. / Ferrara, Luana; Wallat, Gregor Dominik; Moynie, Lucile; Dhanasekar, Naresh; Aliouane, Soumeya; Acosta-Gutiérrez, Silvia; Pagès, Jean-Marie; Bolla, Jean-Michel; Winterhalter, Mathias; Ceccarelli, Matteo; Naismith, James H.

In: Journal of Molecular Biology, Vol. 428, No. 22, 06.11.2016, p. 4528-4543.

Research output: Contribution to journalArticlepeer-review

Harvard

Ferrara, L, Wallat, GD, Moynie, L, Dhanasekar, N, Aliouane, S, Acosta-Gutiérrez, S, Pagès, J-M, Bolla, J-M, Winterhalter, M, Ceccarelli, M & Naismith, JH 2016, 'MOMP from Campylobacter jejuni is a trimer of 18-stranded β–barrel monomers with a Ca2+ ion bound at the constriction zone', Journal of Molecular Biology, vol. 428, no. 22, pp. 4528-4543. https://doi.org/10.1016/j.jmb.2016.09.021

APA

Ferrara, L., Wallat, G. D., Moynie, L., Dhanasekar, N., Aliouane, S., Acosta-Gutiérrez, S., Pagès, J-M., Bolla, J-M., Winterhalter, M., Ceccarelli, M., & Naismith, J. H. (2016). MOMP from Campylobacter jejuni is a trimer of 18-stranded β–barrel monomers with a Ca2+ ion bound at the constriction zone. Journal of Molecular Biology, 428(22), 4528-4543. https://doi.org/10.1016/j.jmb.2016.09.021

Vancouver

Ferrara L, Wallat GD, Moynie L, Dhanasekar N, Aliouane S, Acosta-Gutiérrez S et al. MOMP from Campylobacter jejuni is a trimer of 18-stranded β–barrel monomers with a Ca2+ ion bound at the constriction zone. Journal of Molecular Biology. 2016 Nov 6;428(22):4528-4543. https://doi.org/10.1016/j.jmb.2016.09.021

Author

Ferrara, Luana ; Wallat, Gregor Dominik ; Moynie, Lucile ; Dhanasekar, Naresh ; Aliouane, Soumeya ; Acosta-Gutiérrez, Silvia ; Pagès, Jean-Marie ; Bolla, Jean-Michel ; Winterhalter, Mathias ; Ceccarelli, Matteo ; Naismith, James H. / MOMP from Campylobacter jejuni is a trimer of 18-stranded β–barrel monomers with a Ca2+ ion bound at the constriction zone. In: Journal of Molecular Biology. 2016 ; Vol. 428, No. 22. pp. 4528-4543.

Bibtex - Download

@article{042dd2cf06604541b97c65c4c8803542,
title = "MOMP from Campylobacter jejuni is a trimer of 18-stranded β–barrel monomers with a Ca2+ ion bound at the constriction zone",
abstract = "The Gram-negative organism Campylobacter jejuni is the major cause of food poisoning. Unlike Escherichia coli which has two major porins, OmpC and OmpF, C. jejuni has one, termed major outer membrane protein (MOMP) through which nutrients and antibiotics transit. We report the 2.1-{\AA} crystal structure of C. jejuni MOMP expressed in E. coli and a lower resolution but otherwise identical structure purified directly from C. jejuni. The 2.1-{\AA} resolution structure of recombinant MOMP showed that although the protein has timeric arrangement similar to OmpC, it is an18-stranded not 16-stranded β-barrel. The structure has identified a Ca2+ bound at the constriction zone, which molecular dynamics and single channel experiments suggest is functionally significant. The water filled channel of MOMP has a narrow constriction zone and single molecule studies show a monomeric conductivity of 0.7 ± 0.2 nS and a trimeric conductance of 2.2 ± 0.2 nS. The ion neutralizes negative charges at the constriction zone reducing the transverse electric field and reversing ion selectivity. Modelling of the transit of ciprofloxacin, an antibiotic of choice for treating Campylobacter infection, through the pore of MOMP reveals a trajectory that is dependent upon the presence metal ion.",
keywords = "Campylobacter, Outer membrane proteins, Antibiotic resistance, β-barrel, porins",
author = "Luana Ferrara and Wallat, {Gregor Dominik} and Lucile Moynie and Naresh Dhanasekar and Soumeya Aliouane and Silvia Acosta-Guti{\'e}rrez and Jean-Marie Pag{\`e}s and Jean-Michel Bolla and Mathias Winterhalter and Matteo Ceccarelli and Naismith, {James H.}",
note = "LGMF and SG are funded by EU FP7-PEOPLE-2013-ITN Translocation network Nr. 607694. The research leading to these results was conducted as part of the Translocation consortium (www.translocation.com) and has received support from the Innovative Medicines Initiatives Joint Undertaking under Grant Agreement n°115525, resources which are composed of financial contribution from the European Union{\textquoteright}s seventh framework programme (FP7/2007-2013) and EFPIA companies in kind contribution. JHN is Royal Society Wolfson Merit Award holder, Senior Investigator Wellcome Trust (WT100209MA) and Chinese Academy of Science 1000 Talent Scholar.",
year = "2016",
month = nov,
day = "6",
doi = "10.1016/j.jmb.2016.09.021",
language = "English",
volume = "428",
pages = "4528--4543",
journal = "Journal of Molecular Biology",
issn = "0022-2836",
publisher = "ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD",
number = "22",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - MOMP from Campylobacter jejuni is a trimer of 18-stranded β–barrel monomers with a Ca2+ ion bound at the constriction zone

AU - Ferrara, Luana

AU - Wallat, Gregor Dominik

AU - Moynie, Lucile

AU - Dhanasekar, Naresh

AU - Aliouane, Soumeya

AU - Acosta-Gutiérrez, Silvia

AU - Pagès, Jean-Marie

AU - Bolla, Jean-Michel

AU - Winterhalter, Mathias

AU - Ceccarelli, Matteo

AU - Naismith, James H.

N1 - LGMF and SG are funded by EU FP7-PEOPLE-2013-ITN Translocation network Nr. 607694. The research leading to these results was conducted as part of the Translocation consortium (www.translocation.com) and has received support from the Innovative Medicines Initiatives Joint Undertaking under Grant Agreement n°115525, resources which are composed of financial contribution from the European Union’s seventh framework programme (FP7/2007-2013) and EFPIA companies in kind contribution. JHN is Royal Society Wolfson Merit Award holder, Senior Investigator Wellcome Trust (WT100209MA) and Chinese Academy of Science 1000 Talent Scholar.

PY - 2016/11/6

Y1 - 2016/11/6

N2 - The Gram-negative organism Campylobacter jejuni is the major cause of food poisoning. Unlike Escherichia coli which has two major porins, OmpC and OmpF, C. jejuni has one, termed major outer membrane protein (MOMP) through which nutrients and antibiotics transit. We report the 2.1-Å crystal structure of C. jejuni MOMP expressed in E. coli and a lower resolution but otherwise identical structure purified directly from C. jejuni. The 2.1-Å resolution structure of recombinant MOMP showed that although the protein has timeric arrangement similar to OmpC, it is an18-stranded not 16-stranded β-barrel. The structure has identified a Ca2+ bound at the constriction zone, which molecular dynamics and single channel experiments suggest is functionally significant. The water filled channel of MOMP has a narrow constriction zone and single molecule studies show a monomeric conductivity of 0.7 ± 0.2 nS and a trimeric conductance of 2.2 ± 0.2 nS. The ion neutralizes negative charges at the constriction zone reducing the transverse electric field and reversing ion selectivity. Modelling of the transit of ciprofloxacin, an antibiotic of choice for treating Campylobacter infection, through the pore of MOMP reveals a trajectory that is dependent upon the presence metal ion.

AB - The Gram-negative organism Campylobacter jejuni is the major cause of food poisoning. Unlike Escherichia coli which has two major porins, OmpC and OmpF, C. jejuni has one, termed major outer membrane protein (MOMP) through which nutrients and antibiotics transit. We report the 2.1-Å crystal structure of C. jejuni MOMP expressed in E. coli and a lower resolution but otherwise identical structure purified directly from C. jejuni. The 2.1-Å resolution structure of recombinant MOMP showed that although the protein has timeric arrangement similar to OmpC, it is an18-stranded not 16-stranded β-barrel. The structure has identified a Ca2+ bound at the constriction zone, which molecular dynamics and single channel experiments suggest is functionally significant. The water filled channel of MOMP has a narrow constriction zone and single molecule studies show a monomeric conductivity of 0.7 ± 0.2 nS and a trimeric conductance of 2.2 ± 0.2 nS. The ion neutralizes negative charges at the constriction zone reducing the transverse electric field and reversing ion selectivity. Modelling of the transit of ciprofloxacin, an antibiotic of choice for treating Campylobacter infection, through the pore of MOMP reveals a trajectory that is dependent upon the presence metal ion.

KW - Campylobacter

KW - Outer membrane proteins

KW - Antibiotic resistance

KW - β-barrel

KW - porins

UR - http://www.sciencedirect.com/science/article/pii/S0022283616304016#appd001

U2 - 10.1016/j.jmb.2016.09.021

DO - 10.1016/j.jmb.2016.09.021

M3 - Article

VL - 428

SP - 4528

EP - 4543

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

SN - 0022-2836

IS - 22

ER -

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