Crystal Structure of the Parasporin-2 Bacillus thuringiensis Toxin That Recognizes Cancer Cells

Akiba, T.; Abe, Yuichi; Kitada, Sakae; Kusaka, Yoshitomo; Ito, Akio; Ichimatsu, Tokio; Katayama, Hideki; Akao, Tetsuyuki; Higuchi, Kazuhiko; Mizuki, Eiichi; Ohba, Michio; Kanai, Ryuzi; Harata, Kazuaki

doi:10.1016/j.jmb.2008.12.002

Cited by 92 publications

(117 citation statements)

References 64 publications

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“…Ser/Thr tracks have also been reported in parasporin 30 and lysenin 31 , two members of the aerolysin super-family, suggesting that they are essential for pore formation.…”

Section: Discussionmentioning

confidence: 87%

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

et al. 2013

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(2013) 'Molecular assembly of the aerolysin pore reveals a swirling membrane-insertion mechanism.', Nature chemical biology., 9 (10). pp. 623-629. Further information on publisher's website:https://doi.org/10.1038/nchembio.1312Publisher's copyright statement:Additional information: Use policyThe full-text may be used and/or reproduced, and given to third parties in any format or medium, without prior permission or charge, for personal research or study, educational, or not-for-prot purposes provided that:• a full bibliographic reference is made to the original source • a link is made to the metadata record in DRO • the full-text is not changed in any way The full-text must not be sold in any format or medium without the formal permission of the copyright holders.Please consult the full DRO policy for further details. AbstractAerolysin is the founding member of a super-family of ß-pore forming toxins for which the pore structure is unknown. We have combined X-ray crystallography, cryo-electron microscopy (EM), molecular dynamics and computational modeling to determine the structures of aerolysin mutants in their monomeric and heptameric forms, trapped at various stages of the pore formation process. A dynamic modeling approach based on swarm intelligence was applied whereby the intrinsic flexibility of aerolysin extracted from new X-ray structures was utilized to fully exploit the cryo-EM spatial restraints. Using this integrated strategy, we obtained a radically new arrangement of the prepore conformation and a near-atomistic structure of the aerolysin pore, which is fully consistent with all biochemical data available so far. Upon transition from the prepore to pore, the aerolysin heptamer shows a unique concerted swirling movement, accompanied by a vertical collapse of the complex, ultimately leading to the insertion of a transmembrane ß-barrel.3

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“…Ser/Thr tracks have also been reported in parasporin 30 and lysenin 31 , two members of the aerolysin super-family, suggesting that they are essential for pore formation.…”

Section: Discussionmentioning

confidence: 87%

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

et al. 2013

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“…Cry21 The structures of the insecticidal toxins BinB (PDB 3WA1 (Srisucharitpanit et al, 2014)), Cry35 (PDB 4JP0 (Kelker et al, 2014)), Cry23 (PDB 4RHZ), Cry45 (PDB 2D42 (Akiba et al, 2006)), Cry46 (PDB 2ZTB (Akiba et al, 2009)) and Cry51 (PDB 4PKM (Xu et al, 2015)) are…”

Section: Cry1mentioning

confidence: 99%

Structural classification of insecticidal proteins – Towards an in silico characterisation of novel toxins

Berry

Crickmore

2017

Journal of Invertebrate Pathology

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Article (Accepted Version) http://sro.sussex.ac.uk Berry, Colin and Crickmore, Neil (2017) Structural classification of insecticidal proteins -towards an in silico characterization of novel toxins. Journal of Invertebrate Pathology, 142. pp. 16-22. ISSN 0022-2011 This version is available from Sussex Research Online: http://sro.sussex.ac.uk/62164/ This document is made available in accordance with publisher policies and may differ from the published version or from the version of record. If you wish to cite this item you are advised to consult the publisher's version. Please see the URL above for details on accessing the published version. Copyright and reuse:Sussex Research Online is a digital repository of the research output of the University.Copyright and all moral rights to the version of the paper presented here belong to the individual author(s) and/or other copyright owners. To the extent reasonable and practicable, the material made available in SRO has been checked for eligibility before being made available.Copies of full text items generally can be reproduced, displayed or performed and given to third parties in any format or medium for personal research or study, educational, or not-for-profit purposes without prior permission or charge, provided that the authors, title and full bibliographic details are credited, a hyperlink and/or URL is given for the original metadata page and the content is not changed in any way. This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. Accepted Manuscript Abstract:The increasing rate of discovery of new toxins with potential for the control of invertebrate pests through next generation sequencing, presents challenges for the identification of the best candidates for further development. A consideration of structural similarities between the different toxins suggest that they may be functionally less diverse than their low sequence similarities might predict. This is encouraging from the prospective of being able to use computational tools to predict toxin targets from their sequences, however more structure/function data are still required to reliably inform such predictions.Introduction:

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“…The crystal structure of parasporin 2 was determined (PDB 2ZTB); it is a beta hairpin toxin ( Figure 30.3) that has some similarities to the Epsilon toxin from Clostridium perfringens [21].…”

Section: Other Cry Toxinsmentioning

confidence: 99%

Mechanism of action of Bacillus thuringiensis insecticidal toxins and their use in the control of insect pests

Bravo

Castro

Sánchez

et al. 2015

The Comprehensive Sourcebook of Bacterial Protein Toxins

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Crystal Structure of the Parasporin-2 Bacillus thuringiensis Toxin That Recognizes Cancer Cells

Cited by 92 publications

References 64 publications

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

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

Structural classification of insecticidal proteins – Towards an in silico characterisation of novel toxins

Mechanism of action of Bacillus thuringiensis insecticidal toxins and their use in the control of insect pests

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