1x75

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(New page: 200px<br /><applet load="1x75" size="450" color="white" frame="true" align="right" spinBox="true" caption="1x75, resolution 2.8&Aring;" /> '''CcdB:GyrA14 complex''...)
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[[Image:1x75.gif|left|200px]]<br /><applet load="1x75" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1x75.gif|left|200px]]<br /><applet load="1x75" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1x75, resolution 2.8&Aring;" />
caption="1x75, resolution 2.8&Aring;" />
'''CcdB:GyrA14 complex'''<br />
'''CcdB:GyrA14 complex'''<br />
==Overview==
==Overview==
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Gyrase is an ubiquitous bacterial enzyme that is responsible for, disentangling DNA during DNA replication and transcription. It is the, target of the toxin CcdB, a paradigm for plasmid addiction systems and, related bacterial toxin-antitoxin systems. The crystal structure of CcdB, and the dimerization domain of the A subunit of gyrase (GyrA14) dictates, an open conformation for the catalytic domain of gyrase when CcdB is, bound. The action of CcdB is one of a wedge that stabilizes a dead-end, covalent gyrase:DNA adduct. Although CcdB and GyrA14 form a globally, symmetric complex where the two 2-fold axes of both dimers align, the, complex is asymmetric in its details. At the centre of the interaction, site, the Trp99 pair of CcdB stacks with the Arg462 pair of GyrA14, explaining why the Arg462Cys mutation in the A subunit of gyrase confers, resistance to CcdB. Overexpression of GyrA14 protects Escherichia coli, cells against CcdB, mimicking the action of the antidote CcdA.
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Gyrase is an ubiquitous bacterial enzyme that is responsible for disentangling DNA during DNA replication and transcription. It is the target of the toxin CcdB, a paradigm for plasmid addiction systems and related bacterial toxin-antitoxin systems. The crystal structure of CcdB and the dimerization domain of the A subunit of gyrase (GyrA14) dictates an open conformation for the catalytic domain of gyrase when CcdB is bound. The action of CcdB is one of a wedge that stabilizes a dead-end covalent gyrase:DNA adduct. Although CcdB and GyrA14 form a globally symmetric complex where the two 2-fold axes of both dimers align, the complex is asymmetric in its details. At the centre of the interaction site, the Trp99 pair of CcdB stacks with the Arg462 pair of GyrA14, explaining why the Arg462Cys mutation in the A subunit of gyrase confers resistance to CcdB. Overexpression of GyrA14 protects Escherichia coli cells against CcdB, mimicking the action of the antidote CcdA.
==About this Structure==
==About this Structure==
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1X75 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/DNA_topoisomerase_(ATP-hydrolyzing) DNA topoisomerase (ATP-hydrolyzing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.99.1.3 5.99.1.3] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1X75 OCA].
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1X75 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/DNA_topoisomerase_(ATP-hydrolyzing) DNA topoisomerase (ATP-hydrolyzing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.99.1.3 5.99.1.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X75 OCA].
==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Dao-Thi, M.H.]]
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[[Category: Dao-Thi, M H.]]
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[[Category: Genst, E.De.]]
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[[Category: Genst, E De.]]
[[Category: Loris, R.]]
[[Category: Loris, R.]]
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[[Category: Melderen, L.Van.]]
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[[Category: Melderen, L Van.]]
[[Category: Wyns, L.]]
[[Category: Wyns, L.]]
[[Category: bacterial cell death]]
[[Category: bacterial cell death]]
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[[Category: topoisomerase]]
[[Category: topoisomerase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:52:26 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:51:42 2008''

Revision as of 13:51, 21 February 2008


1x75, resolution 2.8Å

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CcdB:GyrA14 complex

Overview

Gyrase is an ubiquitous bacterial enzyme that is responsible for disentangling DNA during DNA replication and transcription. It is the target of the toxin CcdB, a paradigm for plasmid addiction systems and related bacterial toxin-antitoxin systems. The crystal structure of CcdB and the dimerization domain of the A subunit of gyrase (GyrA14) dictates an open conformation for the catalytic domain of gyrase when CcdB is bound. The action of CcdB is one of a wedge that stabilizes a dead-end covalent gyrase:DNA adduct. Although CcdB and GyrA14 form a globally symmetric complex where the two 2-fold axes of both dimers align, the complex is asymmetric in its details. At the centre of the interaction site, the Trp99 pair of CcdB stacks with the Arg462 pair of GyrA14, explaining why the Arg462Cys mutation in the A subunit of gyrase confers resistance to CcdB. Overexpression of GyrA14 protects Escherichia coli cells against CcdB, mimicking the action of the antidote CcdA.

About this Structure

1X75 is a Protein complex structure of sequences from Escherichia coli. Active as DNA topoisomerase (ATP-hydrolyzing), with EC number 5.99.1.3 Full crystallographic information is available from OCA.

Reference

Molecular basis of gyrase poisoning by the addiction toxin CcdB., Dao-Thi MH, Van Melderen L, De Genst E, Afif H, Buts L, Wyns L, Loris R, J Mol Biol. 2005 May 20;348(5):1091-102. Epub 2005 Apr 7. PMID:15854646

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