2iif
From Proteopedia
(New page: 200px<br /><applet load="2iif" size="450" color="white" frame="true" align="right" spinBox="true" caption="2iif, resolution 2.720Å" /> '''single chain Integr...) |
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| - | [[Image:2iif.gif|left|200px]]<br /><applet load="2iif" size=" | + | [[Image:2iif.gif|left|200px]]<br /><applet load="2iif" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2iif, resolution 2.720Å" /> | caption="2iif, resolution 2.720Å" /> | ||
'''single chain Integration Host Factor mutant protein (scIHF2-K45aE) in complex with DNA'''<br /> | '''single chain Integration Host Factor mutant protein (scIHF2-K45aE) in complex with DNA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Architectural proteins that reconfigure the paths of DNA segments are | + | 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== | ==About this Structure== | ||
| - | 2IIF 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 MN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2IIF 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=2IIF OCA]. |
==Reference== | ==Reference== | ||
| - | A | + | 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: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bao, Q.]] | [[Category: Bao, Q.]] | ||
| - | [[Category: Davey, C | + | [[Category: Davey, C A.]] |
[[Category: Droege, P.]] | [[Category: Droege, P.]] | ||
[[Category: MN]] | [[Category: MN]] | ||
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[[Category: u-turn]] | [[Category: u-turn]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:53:03 2008'' |
Revision as of 15:53, 21 February 2008
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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 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 Thu Feb 21 17:53:03 2008
Categories: Escherichia coli | Single protein | Bao, Q. | Davey, C A. | Droege, P. | MN | Bending | Divalent | Dna kinking | Intercalation | Metal | U-turn
