1osl: Difference between revisions
New page: left|200px<br /><applet load="1osl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1osl" /> '''Solution structure of a dimeric lactose DNA-... |
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'''Solution structure of a dimeric lactose DNA-binding domain complexed to a nonspecific DNA sequence'''<br /> | '''Solution structure of a dimeric lactose DNA-binding domain complexed to a nonspecific DNA sequence'''<br /> | ||
==Overview== | ==Overview== | ||
Interaction of regulatory DNA binding proteins with their target sites is | Interaction of regulatory DNA binding proteins with their target sites is usually preceded by binding to nonspecific DNA. This speeds up the search for the target site by several orders of magnitude. We report the solution structure and dynamics of the complex of a dimeric lac repressor DNA binding domain with nonspecific DNA. The same set of residues can switch roles from a purely electrostatic interaction with the DNA backbone in the nonspecific complex to a highly specific binding mode with the base pairs of the cognate operator sequence. The protein-DNA interface of the nonspecific complex is flexible on biologically relevant time scales that may assist in the rapid and efficient finding of the target site. | ||
==About this Structure== | ==About this Structure== | ||
1OSL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | 1OSL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OSL OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Boelens, R.]] | [[Category: Boelens, R.]] | ||
[[Category: Bonvin, A | [[Category: Bonvin, A M.J J.]] | ||
[[Category: Kalodimos, C | [[Category: Kalodimos, C G.]] | ||
[[Category: Kaptein, R.]] | [[Category: Kaptein, R.]] | ||
[[Category: lac repressor]] | [[Category: lac repressor]] | ||
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[[Category: protein-dna complex]] | [[Category: protein-dna complex]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:21:06 2008'' | ||
Revision as of 15:21, 21 February 2008
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Solution structure of a dimeric lactose DNA-binding domain complexed to a nonspecific DNA sequence
OverviewOverview
Interaction of regulatory DNA binding proteins with their target sites is usually preceded by binding to nonspecific DNA. This speeds up the search for the target site by several orders of magnitude. We report the solution structure and dynamics of the complex of a dimeric lac repressor DNA binding domain with nonspecific DNA. The same set of residues can switch roles from a purely electrostatic interaction with the DNA backbone in the nonspecific complex to a highly specific binding mode with the base pairs of the cognate operator sequence. The protein-DNA interface of the nonspecific complex is flexible on biologically relevant time scales that may assist in the rapid and efficient finding of the target site.
About this StructureAbout this Structure
1OSL is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
Structure and flexibility adaptation in nonspecific and specific protein-DNA complexes., Kalodimos CG, Biris N, Bonvin AM, Levandoski MM, Guennuegues M, Boelens R, Kaptein R, Science. 2004 Jul 16;305(5682):386-9. PMID:15256668
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