1ub4
From Proteopedia
(New page: 200px<br /><applet load="1ub4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ub4, resolution 1.70Å" /> '''crystal structure of...) |
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- | [[Image:1ub4.gif|left|200px]]<br /><applet load="1ub4" size=" | + | [[Image:1ub4.gif|left|200px]]<br /><applet load="1ub4" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ub4, resolution 1.70Å" /> | caption="1ub4, resolution 1.70Å" /> | ||
'''crystal structure of MazEF complex'''<br /> | '''crystal structure of MazEF complex'''<br /> | ||
==Overview== | ==Overview== | ||
- | A structure of the Escherichia coli chromosomal MazE/MazF addiction module | + | 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== | ==About this Structure== | ||
- | 1UB4 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | + | 1UB4 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UB4 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
- | [[Category: Burley, S | + | [[Category: Burley, S K.]] |
[[Category: Hanaoka, F.]] | [[Category: Hanaoka, F.]] | ||
[[Category: Kamada, K.]] | [[Category: Kamada, K.]] | ||
- | [[Category: NYSGXRC, New | + | [[Category: NYSGXRC, New York Structural GenomiX Research Consortium.]] |
[[Category: addiction module]] | [[Category: addiction module]] | ||
[[Category: antidote]] | [[Category: antidote]] | ||
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[[Category: toxin]] | [[Category: toxin]] | ||
- | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:22:31 2008'' |
Revision as of 13:22, 21 February 2008
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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
Page seeded by OCA on Thu Feb 21 15:22:31 2008
Categories: Escherichia coli | Protein complex | Burley, S K. | Hanaoka, F. | Kamada, K. | NYSGXRC, New York Structural GenomiX Research Consortium. | Addiction module | Antidote | New york structural genomix research consortium | Nysgxrc | Post-segregation | Programmed cell death | Protein structure initiative | Psi | Structural genomics | Toxin