2h3c

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[[Image:2h3c.gif|left|200px]]
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{{Structure
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|LIGAND= <scene name='pdbligand=DA:2&#39;-DEOXYADENOSINE-5&#39;-MONOPHOSPHATE'>DA</scene>, <scene name='pdbligand=DC:2&#39;-DEOXYCYTIDINE-5&#39;-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DG:2&#39;-DEOXYGUANOSINE-5&#39;-MONOPHOSPHATE'>DG</scene>, <scene name='pdbligand=DT:THYMIDINE-5&#39;-MONOPHOSPHATE'>DT</scene>
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{{STRUCTURE_2h3c| PDB=2h3c | SCENE= }}
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|RELATEDENTRY=[[2h3a|2H3A]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2h3c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h3c OCA], [http://www.ebi.ac.uk/pdbsum/2h3c PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2h3c RCSB]</span>
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'''Structural basis for nucleic acid and toxin recognition of the bacterial antitoxin CcdA'''
'''Structural basis for nucleic acid and toxin recognition of the bacterial antitoxin CcdA'''
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[[Category: Respondek, M.]]
[[Category: Respondek, M.]]
[[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 Sun May 4 05:49:01 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:24:49 2008''
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Revision as of 02:49, 4 May 2008

Template:STRUCTURE 2h3c

Structural basis for nucleic acid and toxin recognition of the bacterial antitoxin CcdA


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

2H3C 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 Sun May 4 05:49:01 2008

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