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Literature DB >> 24045807

Structural biology: Torqueing about pores.

James C Whisstock¹, Michelle A Dunstone.

Abstract

Cryo-EM, crystallography, biochemical experiments and computational approaches have been used to study different intermediate states of the Aeromonas hydrophila toxin aerolysin en route to pore formation. These results reveal that an unexpected and marked rotation of the core aerolysin machinery is required to unleash the membrane-spanning regions.

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Year: 2013 PMID： 24045807 DOI： 10.1038/nchembio.1341

Source DB: PubMed Journal: Nat Chem Biol ISSN： 1552-4450 Impact factor: 15.040

10 in total

1. Conversion of a transmembrane to a water-soluble protein complex by a single point mutation.

Authors: Yulia Tsitrin; Craig J Morton; Catherine el-Bez; Patrick Paumard; Marie-Claire Velluz; Marc Adrian; Jacques Dubochet; Michael W Parker; Salvatore Lanzavecchia; F G van der Goot
Journal: Nat Struct Biol Date: 2002-10

2. A rivet model for channel formation by aerolysin-like pore-forming toxins.

Authors: Ioan Iacovache; Patrick Paumard; Holger Scheib; Claire Lesieur; Naomi Sakai; Stefan Matile; Michael W Parker; F Gisou van der Goot
Journal: EMBO J Date: 2006-01-19 Impact factor: 11.598

3. Macromolecular symmetric assembly prediction using swarm intelligence dynamic modeling.

Authors: Matteo T Degiacomi; Matteo Dal Peraro
Journal: Structure Date: 2013-07-02 Impact factor: 5.006

4. Molecular assembly of the aerolysin pore reveals a swirling membrane-insertion mechanism.

Authors: Matteo T Degiacomi; Ioan Iacovache; Lucile Pernot; Mohamed Chami; Misha Kudryashev; Henning Stahlberg; F Gisou van der Goot; Matteo Dal Peraro
Journal: Nat Chem Biol Date: 2013-08-04 Impact factor: 15.040

5. The glycosylphosphatidylinositol-anchored surface glycoprotein Thy-1 is a receptor for the channel-forming toxin aerolysin.

Authors: K L Nelson; S M Raja; J T Buckley
Journal: J Biol Chem Date: 1997-05-02 Impact factor: 5.157

1 in total

Review 1. Structural insights into Bacillus thuringiensis Cry, Cyt and parasporin toxins.

Authors: Chengchen Xu; Bi-Cheng Wang; Ziniu Yu; Ming Sun
Journal: Toxins (Basel) Date: 2014-09-16 Impact factor: 4.546

1 in total

Structural biology: Torqueing about pores.

1. Conversion of a transmembrane to a water-soluble protein complex by a single point mutation.

2. A rivet model for channel formation by aerolysin-like pore-forming toxins.

3. Macromolecular symmetric assembly prediction using swarm intelligence dynamic modeling.

4. Molecular assembly of the aerolysin pore reveals a swirling membrane-insertion mechanism.

5. The glycosylphosphatidylinositol-anchored surface glycoprotein Thy-1 is a receptor for the channel-forming toxin aerolysin.

6. Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states.

7. The aerolysin membrane channel is formed by heptamerization of the monomer.

8. Dual chaperone role of the C-terminal propeptide in folding and oligomerization of the pore-forming toxin aerolysin.

9. Extending the aerolysin family: from bacteria to vertebrates.

10. A pore-forming toxin interacts with a GPI-anchored protein and causes vacuolation of the endoplasmic reticulum.

Review 1. Structural insights into Bacillus thuringiensis Cry, Cyt and parasporin toxins.