2iif
From Proteopedia
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single chain Integration Host Factor mutant protein (scIHF2-K45aE) in complex with DNA
Overview
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.
About this Structure
2IIF is a Single protein structure of sequence from Escherichia coli with MN as ligand. Full crystallographic information is available from OCA.
Reference
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:17276457
Page seeded by OCA on Wed Nov 21 12:20:12 2007
Categories: Escherichia coli | Single protein | Bao, Q. | Davey, C.A. | Droege, P. | MN | Bending | Divalent | Dna kinking | Intercalation | Metal | U-turn
