2adn

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[[Image:2adn.gif|left|200px]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2adn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2adn OCA], [http://www.ebi.ac.uk/pdbsum/2adn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2adn RCSB]</span>
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'''Solution structure of the bacterial antitoxin CcdA: Implications for DNA and toxin binding'''
'''Solution structure of the bacterial antitoxin CcdA: Implications for DNA and toxin binding'''
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[[Category: VanMelderen, L.]]
[[Category: VanMelderen, L.]]
[[Category: Zangger, K.]]
[[Category: Zangger, K.]]
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[[Category: ribbon-helix-helix]]
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[[Category: Ribbon-helix-helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:54:51 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:51:10 2008''
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Revision as of 15:54, 3 May 2008

Template:STRUCTURE 2adn

Solution structure of the bacterial antitoxin CcdA: Implications for DNA and toxin binding


Overview

Toxin-antitoxin systems are highly abundant in plasmids and bacterial chromosomes. They ensure plasmid maintenance by killing bacteria that have lost the plasmid. Their expression is autoregulated at the level of transcription. Here, we present the solution structure of CcdA, the antitoxin of the ccd system, as a free protein (16.7 kDa) and in complex with its cognate DNA (25.3 kDa). CcdA is composed of two distinct and independent domains: the N-terminal domain, responsible for DNA binding, which establishes a new family of the ribbon-helix-helix fold and the C-terminal region, which is responsible for the interaction with the toxin CcdB. The C-terminal domain is intrinsically unstructured and forms a tight complex with the toxin. We show that CcdA specifically recognizes a 6 bp palindromic DNA sequence within the operator-promoter (OP) region of the ccd operon and binds to DNA by insertion of the positively charged N-terminal beta-sheet into the major groove. The binding of up to three CcdA dimers to a 33mer DNA of its operator-promoter region was studied by NMR spectroscopy, isothermal titration calorimetry and single point mutation. The highly flexible C-terminal region of free CcdA explains its susceptibility to proteolysis by the Lon ATP-dependent protease.

About this Structure

2ADN is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structural basis for nucleic acid and toxin recognition of the bacterial antitoxin CcdA., Madl T, Van Melderen L, Mine N, Respondek M, Oberer M, Keller W, Khatai L, Zangger K, J Mol Biol. 2006 Nov 24;364(2):170-85. Epub 2006 Sep 1. PMID:17007877 Page seeded by OCA on Sat May 3 18:54:51 2008

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