Structure of a Tc holotoxin pore provides insights into the translocation mechanism.


Journal

Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876

Informations de publication

Date de publication:
12 11 2019
Historique:
pubmed: 2 11 2019
medline: 2 4 2020
entrez: 1 11 2019
Statut: ppublish

Résumé

Tc toxins are modular toxin systems of insect and human pathogenic bacteria. They are composed of a 1.4-MDa pentameric membrane translocator (TcA) and a 250-kDa cocoon (TcB and TcC) encapsulating the 30-kDa toxic enzyme (C terminus of TcC). Binding of Tc toxins to target cells and a pH shift trigger the conformational transition from the soluble prepore state to the membrane-embedded pore. Subsequently, the toxic enzyme is translocated and released into the cytoplasm. A high-resolution structure of a holotoxin embedded in membranes is missing, leaving open the question of whether TcB-TcC has an influence on the conformational transition of TcA. Here we show in atomic detail a fully assembled 1.7-MDa Tc holotoxin complex from

Identifiants

pubmed: 31666324
pii: 1909821116
doi: 10.1073/pnas.1909821116
pmc: PMC6859359
doi:

Substances chimiques

Bacterial Toxins 0
ADP Ribose Transferases EC 2.4.2.-

Banques de données

PDB
['6SUE', '6SUF']

Types de publication

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

Langues

eng

Sous-ensembles de citation

IM

Pagination

23083-23090

Déclaration de conflit d'intérêts

The authors declare no competing interest.

Références

J Struct Biol. 2013 Nov;184(2):261-70
pubmed: 23999189
J Biol Chem. 2016 Feb 12;291(7):3658-67
pubmed: 26663081
Nat Commun. 2018 Mar 14;9(1):1079
pubmed: 29540701
Cell Microbiol. 2014 Apr;16(4):490-503
pubmed: 24138221
Acta Crystallogr D Biol Crystallogr. 2010 Jan;66(Pt 1):12-21
pubmed: 20057044
Nat Biotechnol. 2013 Jun;31(6):510-21
pubmed: 23752438
Appl Environ Microbiol. 2000 Aug;66(8):3310-29
pubmed: 10919786
Ultramicroscopy. 2014 May;140:9-19
pubmed: 24562077
J Vis Exp. 2017 May 16;(123):
pubmed: 28570515
J Am Soc Mass Spectrom. 2015 Jan;26(1):83-97
pubmed: 25261217
Nat Methods. 2015 Oct;12(10):943-6
pubmed: 26280328
Nat Methods. 2015 Apr;12(4):361-365
pubmed: 25707030
BMC Bioinformatics. 2015 Apr 16;16:119
pubmed: 25888118
Nature. 2015 Jan 1;517(7532):39-43
pubmed: 25470059
Acta Crystallogr D Struct Biol. 2018 Jun 1;74(Pt 6):531-544
pubmed: 29872004
Nature. 2013 Sep 26;501(7468):547-50
pubmed: 23913273
Mol Cell. 2018 May 3;70(3):545-552.e9
pubmed: 29706537
Nature. 2015 May 28;521(7553):545-9
pubmed: 25778700
J Am Chem Soc. 2004 Mar 24;126(11):3477-87
pubmed: 15025475
Acta Crystallogr D Biol Crystallogr. 2010 Apr;66(Pt 4):486-501
pubmed: 20383002
Nat Struct Mol Biol. 2016 Oct;23(10):884-890
pubmed: 27571177
Science. 1998 Jun 26;280(5372):2129-32
pubmed: 9641921
Protein Pept Lett. 2002 Aug;9(4):289-94
pubmed: 12144505
J Biol Chem. 2011 Jul 1;286(26):23189-99
pubmed: 21507946
Microbes Infect. 2004 Feb;6(2):229-37
pubmed: 15049334
Nature. 2005 Jan 27;433(7024):377-81
pubmed: 15674282
Cell Mol Life Sci. 2000 May;57(5):828-33
pubmed: 10892346
Cell. 2018 Apr 19;173(3):735-748.e15
pubmed: 29677516
Nature. 2014 Apr 3;508(7494):61-5
pubmed: 24572368
PLoS Pathog. 2013;9(10):e1003644
pubmed: 24098116
Science. 2017 Jul 21;357(6348):273-279
pubmed: 28619716
Science. 2017 Nov 3;358(6363):
pubmed: 29097521
Sci Rep. 2017 Jun 2;7(1):2724
pubmed: 28578412
Science. 2010 Feb 26;327(5969):1139-42
pubmed: 20185726
Appl Environ Microbiol. 2003 Jun;69(6):3344-9
pubmed: 12788735
Nature. 2018 Nov;563(7730):209-213
pubmed: 30232455
Adv Exp Med Biol. 2007;603:247-57
pubmed: 17966421
Nature. 2013 Mar 28;495(7442):520-3
pubmed: 23515159
Nat Methods. 2017 Apr;14(4):331-332
pubmed: 28250466
Trends Microbiol. 2001 Apr;9(4):185-91
pubmed: 11286884
Nat Biotechnol. 2003 Nov;21(11):1307-13
pubmed: 14528314
Infect Immun. 2005 Oct;73(10):6860-7
pubmed: 16177365
Nucleic Acids Res. 2015 Jul 1;43(W1):W362-9
pubmed: 25956653
Structure. 2012 Feb 8;20(2):237-47
pubmed: 22325773
Science. 2005 Jul 29;309(5735):777-81
pubmed: 16051798

Auteurs

Daniel Roderer (D)

Department of Structural Biochemistry, Max Planck Institute of Molecular Physiology, 44227 Dortmund, Germany.

Oliver Hofnagel (O)

Department of Structural Biochemistry, Max Planck Institute of Molecular Physiology, 44227 Dortmund, Germany.

Roland Benz (R)

Department of Life Sciences and Chemistry, Jacobs University Bremen, 28759 Bremen, Germany.

Stefan Raunser (S)

Department of Structural Biochemistry, Max Planck Institute of Molecular Physiology, 44227 Dortmund, Germany; raunser@mpi-dortmund.mpg.de.

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Classifications MeSH