2iie: Difference between revisions

[[Image:2iie.gif|left|200px]]<br /><applet load="2iie" size="350" color="white" frame="true" align="right" spinBox="true"  

Architectural proteins that reconfigure the paths of DNA segments are required for the establishment of functional interfaces in many genomic transactions. A single-chain derivative of the DNA architectural protein integration host factor was found to adopt two stable conformational states in complex with a specific DNA target. In the so-called open state, the degree of protein-induced DNA bending is reduced significantly compared with the closed state. The conformational switch between these states is controlled by divalent metal binding in two electronegative zones arising from the lysine-to-glutamate substitution in the protein body proximal to the phosphate backbone of one DNA arm. We show that this switch can be employed to control the efficiency of site-specific recombination catalyzed by lambda integrase. Introduction of acidic residues at the protein-DNA interface holds potential for the design of metal-mediated switches for the investigation of functional relationships.

2IIE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MN:'>MN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IIE OCA].  

A divalent metal-mediated switch controlling protein-induced DNA bending., Bao Q, Chen H, Liu Y, Yan J, Droge P, Davey CA, J Mol Biol. 2007 Mar 30;367(3):731-40. Epub 2006 Oct 3. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17276457 17276457]

[[Category: Davey, C A.]]

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