Negative charge of the AC-to-Hly linking segment modulates calcium-dependent membrane activities of Bordetella adenylate cyclase toxin.


Journal

Biochimica et biophysica acta. Biomembranes
ISSN: 1879-2642
Titre abrégé: Biochim Biophys Acta Biomembr
Pays: Netherlands
ID NLM: 101731713

Informations de publication

Date de publication:
01 09 2020
Historique:
received: 10 01 2020
revised: 31 03 2020
accepted: 13 04 2020
pubmed: 26 4 2020
medline: 15 12 2020
entrez: 26 4 2020
Statut: ppublish

Résumé

Two distinct conformers of the adenylate cyclase toxin (CyaA) appear to accomplish its two parallel activities within target cell membrane. The translocating conformer would deliver the N-terminal adenylyl cyclase (AC) enzyme domain across plasma membrane into cytosol of cells, while the pore precursor conformer would assemble into oligomeric cation-selective pores and permeabilize cellular membrane. Both toxin activities then involve a membrane-interacting 'AC-to-Hly-linking segment' (residues 400 to 500). Here, we report the NMR structure of the corresponding CyaA

Identifiants

pubmed: 32333856
pii: S0005-2736(20)30141-3
doi: 10.1016/j.bbamem.2020.183310
pii:
doi:

Substances chimiques

Adenylate Cyclase Toxin 0
Lipid Bilayers 0
Cyclic AMP E0399OZS9N
Calcium SY7Q814VUP

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

183310

Informations de copyright

Copyright © 2020 Elsevier B.V. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.

Auteurs

Anna Sukova (A)

Institute of Microbiology of the Czech Academy of Sciences, Videnska 1083, 142 20 Prague, Czech Republic.

Ladislav Bumba (L)

Institute of Microbiology of the Czech Academy of Sciences, Videnska 1083, 142 20 Prague, Czech Republic.

Pavel Srb (P)

Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo namesti. 2, 166 10 Prague, Czech Republic.

Vaclav Veverka (V)

Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo namesti. 2, 166 10 Prague, Czech Republic; Department of Cell Biology, Faculty of Science, Charles University, Vinicna 7, 128 00 Prague, Czech Republic.

Ondrej Stanek (O)

Institute of Microbiology of the Czech Academy of Sciences, Videnska 1083, 142 20 Prague, Czech Republic.

Jana Holubova (J)

Institute of Microbiology of the Czech Academy of Sciences, Videnska 1083, 142 20 Prague, Czech Republic.

Josef Chmelik (J)

Institute of Microbiology of the Czech Academy of Sciences, Videnska 1083, 142 20 Prague, Czech Republic.

Radovan Fiser (R)

Institute of Microbiology of the Czech Academy of Sciences, Videnska 1083, 142 20 Prague, Czech Republic; Department of Genetics and Microbiology, Faculty of Science, Charles University, Vinicna 5, 128 00 Prague, Czech Republic.

Peter Sebo (P)

Institute of Microbiology of the Czech Academy of Sciences, Videnska 1083, 142 20 Prague, Czech Republic.

Jiri Masin (J)

Institute of Microbiology of the Czech Academy of Sciences, Videnska 1083, 142 20 Prague, Czech Republic. Electronic address: masin@biomed.cas.cz.

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Classifications MeSH