1sr4

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{{STRUCTURE_1sr4| PDB=1sr4 | SCENE= }}
{{STRUCTURE_1sr4| PDB=1sr4 | SCENE= }}
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'''Crystal Structure of the Haemophilus ducreyi cytolethal distending toxin'''
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===Crystal Structure of the Haemophilus ducreyi cytolethal distending toxin===
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==Overview==
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The tripartite cytolethal distending toxin (CDT) induces cell cycle arrest and apoptosis in eukaryotic cells. The subunits CdtA and CdtC associate with the nuclease CdtB to form a holotoxin that translocates CdtB into the host cell, where it acts as a genotoxin by creating DNA lesions. Here we show that the crystal structure of the holotoxin from Haemophilus ducreyi reveals that CDT consists of an enzyme of the DNase-I family, bound to two ricin-like lectin domains. CdtA, CdtB and CdtC form a ternary complex with three interdependent molecular interfaces, characterized by globular, as well as extensive non-globular, interactions. The lectin subunits form a deeply grooved, highly aromatic surface that we show to be critical for toxicity. The holotoxin possesses a steric block of the CdtB active site by means of a non-globular extension of the CdtC subunit, and we identify putative DNA binding residues in CdtB that are essential for toxin activity.
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(as it appears on PubMed at http://www.pubmed.gov), where 15164065 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15164065}}
==About this Structure==
==About this Structure==
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[[Category: Toxin]]
[[Category: Toxin]]
[[Category: Virulence]]
[[Category: Virulence]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:03:02 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 16:43:54 2008''

Revision as of 13:43, 27 July 2008

Image:1sr4.png

Template:STRUCTURE 1sr4

Crystal Structure of the Haemophilus ducreyi cytolethal distending toxin

Template:ABSTRACT PUBMED 15164065

About this Structure

1SR4 is a Protein complex structure of sequences from Haemophilus ducreyi. Full crystallographic information is available from OCA.

Reference

Assembly and function of a bacterial genotoxin., Nesic D, Hsu Y, Stebbins CE, Nature. 2004 May 27;429(6990):429-33. PMID:15164065

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