1ub4

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(New page: 200px<br /><applet load="1ub4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ub4, resolution 1.70&Aring;" /> '''crystal structure of...)
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Revision as of 01:51, 21 November 2007

Image:1ub4.gif

1ub4, resolution 1.70Å

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crystal structure of MazEF complex

Overview

A structure of the Escherichia coli chromosomal MazE/MazF addiction module, has been determined at 1.7 A resolution. Addiction modules consist of, stable toxin and unstable antidote proteins that govern bacterial cell, death. MazE (antidote) and MazF (toxin) form a linear heterohexamer, composed of alternating toxin and antidote homodimers, (MazF(2)-MazE(2)-MazF(2)). The MazE homodimer contains a beta barrel from, which two extended C termini project, making interactions with flanking, MazF homodimers that resemble the plasmid-encoded toxins CcdB and Kid. The, MazE/MazF heterohexamer structure documents that the mechanism of, antidote-toxin recognition is common to both chromosomal and plasmid-borne, addiction modules, and provides general molecular insights into toxin, function, antidote degradation in the absence of toxin, and promoter DNA, binding by antidote/toxin complexes.

About this Structure

1UB4 is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Crystal structure of the MazE/MazF complex: molecular bases of antidote-toxin recognition., Kamada K, Hanaoka F, Burley SK, Mol Cell. 2003 Apr;11(4):875-84. PMID:12718874

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