MOMP from Campylobacter jejuni is a trimer of 18-stranded β-barrel monomers with a Ca2 ion bound at the constriction zone.Reportar como inadecuado




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Reference: Ferrara, LG, Wallat, GD, Moynié, L et al., (2016). MOMP from Campylobacter jejuni is a trimer of 18-stranded β-barrel monomers with a Ca(2+) ion bound at the constriction zone. Journal of Molecular Biology, 428 (22), 4528-4543.Citable link to this page:

 

MOMP from Campylobacter jejuni is a trimer of 18-stranded β-barrel monomers with a Ca(2+) 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-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 an 18-stranded, not 16-stranded, β-barrel. The structure has identified a Ca(2+) bound at the constriction zone, which is functionally significant as suggested by molecular dynamics and single-channel experiments. 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. Modeling 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.

Publication status:PublishedPeer Review status:Peer reviewedVersion:Publisher's versionDate of acceptance:2016-09-26 Funder: Seventh Framework Programme   Funder: Innovative Medicines Initiatives Joint Undertaking   Funder: European Federation of Pharmaceutical Industries and Associations   Funder: Royal Society   Funder: Wellcome Trust   Funder: Chinese Academy of Science   Notes:© 2016 The Authors. Published by Elsevier Ltd. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).

Bibliographic Details

Publisher: Elsevier

Publisher Website: http://www.elsevier.com/

Journal: Journal of Molecular Biologysee more from them

Publication Website: http://www.sciencedirect.com/science/journal/00222836

Volume: 428

Issue: 22

Issue Date: 2016-09

pages:4528-4543Identifiers

Doi: https://doi.org/10.1016/j.jmb.2016.09.021

Eissn: 1089-8638

Issn: 0022-2836

Uuid: uuid:63102083-d209-47a1-a275-a04edeea4a3f

Urn: uri:63102083-d209-47a1-a275-a04edeea4a3f

Pubs-id: pubs:699010 Item Description

Type: journal-article;

Language: eng

Version: Publisher's versionKeywords: Campylobacter antibiotic resistance outer membrane proteins porins β-barrel Anti-Bacterial Agents Bacterial Proteins Calcium Campylobacter jejuni Ciprofloxacin Crystallography, X-Ray Escherichia coli Gene Expression Models, Molecular Multiprotein Complexes Porins Protein Conformation Recombinant Proteins

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Autor: Ferrara, LG - - - Wallat, GD - - - Moynié, L - - - Dhanasekar, NN - - - Aliouane, S - - - Acosta-Gutiérrez, S - - - Pagès, JM

Fuente: https://ora.ox.ac.uk/objects/uuid:63102083-d209-47a1-a275-a04edeea4a3f



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