1sr4

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(New page: 200px<br /><applet load="1sr4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sr4, resolution 2.0&Aring;" /> '''Crystal Structure of ...)
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[[Image:1sr4.jpg|left|200px]]<br /><applet load="1sr4" size="350" color="white" frame="true" align="right" spinBox="true"
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caption="1sr4, resolution 2.0&Aring;" />
'''Crystal Structure of the Haemophilus ducreyi cytolethal distending toxin'''<br />
'''Crystal Structure of the Haemophilus ducreyi cytolethal distending toxin'''<br />
==Overview==
==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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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.
==About this Structure==
==About this Structure==
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1SR4 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Haemophilus_ducreyi Haemophilus ducreyi] with BR as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SR4 OCA].
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1SR4 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Haemophilus_ducreyi Haemophilus ducreyi] with <scene name='pdbligand=BR:'>BR</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SR4 OCA].
==Reference==
==Reference==
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[[Category: Hsu, Y.]]
[[Category: Hsu, Y.]]
[[Category: Nesic, D.]]
[[Category: Nesic, D.]]
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[[Category: Stebbins, C.E.]]
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[[Category: Stebbins, C E.]]
[[Category: BR]]
[[Category: BR]]
[[Category: apoptosis]]
[[Category: apoptosis]]
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[[Category: virulence]]
[[Category: virulence]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:35:35 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:04:27 2008''

Revision as of 13:04, 21 February 2008

Image:1sr4.jpg

1sr4, resolution 2.0Å

Drag the structure with the mouse to rotate

Crystal Structure of the Haemophilus ducreyi cytolethal distending toxin

Overview

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.

About this Structure

1SR4 is a Protein complex structure of sequences from Haemophilus ducreyi with as ligand. 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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