1d5y: Difference between revisions

Revision as of 13:13, 21 February 2008

CRYSTAL STRUCTURE OF THE E. COLI ROB TRANSCRIPTION FACTOR IN COMPLEX WITH DNA

OverviewOverview

The Escherichia coli Rob protein is a transcription factor belonging to the AraC/XylS protein family that regulates genes involved in resistance to antibiotics, organic solvents and heavy metals. The genes encoding these proteins are activated by the homologous proteins MarA and SoxS, although the level of activation can vary for the different transcription factors. Here we report a 2.7 A crystal structure of Rob in complex with the micF promoter that reveals an unusual mode of binding to DNA. The Rob-DNA complex differs from the previously reported structure of MarA bound to the mar promoter, in that only one of Rob's dual helix-turn-helix (HTH) motifs engages the major groove of the binding site. Biochemical studies show that sequence specific interactions involving only one of Rob's HTH motifs are sufficient for high affinity binding to DNA. The two different modes of DNA binding seen in crystal structures of Rob and MarA also match the distinctive patterns of DNA protection by AraC at several sites within the pBAD promoter. These and other findings suggest that gene activation by AraC/XylS transcription factors might involve two alternative modes of binding to DNA in different promoter contexts.

About this StructureAbout this Structure

1D5Y is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the Escherichia coli Rob transcription factor in complex with DNA., Kwon HJ, Bennik MH, Demple B, Ellenberger T, Nat Struct Biol. 2000 May;7(5):424-30. PMID:10802742

Page seeded by OCA on Thu Feb 21 12:13:17 2008

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OCA

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-[[Image:1d5y.gif|left|200px]]<br /><applet load="1d5y" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1d5y.gif|left|200px]]<br /><applet load="1d5y" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1d5y, resolution 2.7&Aring;" />
 '''CRYSTAL STRUCTURE OF THE E. COLI ROB TRANSCRIPTION FACTOR IN COMPLEX WITH DNA'''<br />
 ==Overview==
-The Escherichia coli Rob protein is a transcription factor belonging to, the AraC/XylS protein family that regulates genes involved in resistance, to antibiotics, organic solvents and heavy metals. The genes encoding, these proteins are activated by the homologous proteins MarA and SoxS, although the level of activation can vary for the different transcription, factors. Here we report a 2.7 A crystal structure of Rob in complex with, the micF promoter that reveals an unusual mode of binding to DNA. The, Rob-DNA complex differs from the previously reported structure of MarA, bound to the mar promoter, in that only one of Rob's dual helix-turn-helix, (HTH) motifs engages the major groove of the binding site. Biochemical, studies show that sequence specific interactions involving only one of, Rob's HTH motifs are sufficient for high affinity binding to DNA. The two, different modes of DNA binding seen in crystal structures of Rob and MarA, also match the distinctive patterns of DNA protection by AraC at several, sites within the pBAD promoter. These and other findings suggest that gene, activation by AraC/XylS transcription factors might involve two, alternative modes of binding to DNA in different promoter contexts.
+The Escherichia coli Rob protein is a transcription factor belonging to the AraC/XylS protein family that regulates genes involved in resistance to antibiotics, organic solvents and heavy metals. The genes encoding these proteins are activated by the homologous proteins MarA and SoxS, although the level of activation can vary for the different transcription factors. Here we report a 2.7 A crystal structure of Rob in complex with the micF promoter that reveals an unusual mode of binding to DNA. The Rob-DNA complex differs from the previously reported structure of MarA bound to the mar promoter, in that only one of Rob's dual helix-turn-helix (HTH) motifs engages the major groove of the binding site. Biochemical studies show that sequence specific interactions involving only one of Rob's HTH motifs are sufficient for high affinity binding to DNA. The two different modes of DNA binding seen in crystal structures of Rob and MarA also match the distinctive patterns of DNA protection by AraC at several sites within the pBAD promoter. These and other findings suggest that gene activation by AraC/XylS transcription factors might involve two alternative modes of binding to DNA in different promoter contexts.
 ==About this Structure==
-D5Y 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1D5Y OCA].
+D5Y 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=1D5Y OCA].
 ==Reference==
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 [[Category: Escherichia coli]]
 [[Category: Single protein]]
-[[Category: Bennik, M.H.J.]]
+[[Category: Bennik, M H.J.]]
 [[Category: Demple, B.]]
 [[Category: Ellenberger, T.]]
-[[Category: Kwon, H.J.]]
+[[Category: Kwon, H J.]]
 [[Category: dna]]
 [[Category: protein-dna complex]]
 [[Category: rob transcription factor]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:01:56 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:13:17 2008''