1rio

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(New page: 200px<br /><applet load="1rio" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rio, resolution 2.30&Aring;" /> '''Structure of bacteri...)
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[[Image:1rio.gif|left|200px]]<br /><applet load="1rio" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1rio.gif|left|200px]]<br /><applet load="1rio" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1rio, resolution 2.30&Aring;" />
caption="1rio, resolution 2.30&Aring;" />
'''Structure of bacteriophage lambda cI-NTD in complex with sigma-region4 of Thermus aquaticus bound to DNA'''<br />
'''Structure of bacteriophage lambda cI-NTD in complex with sigma-region4 of Thermus aquaticus bound to DNA'''<br />
==Overview==
==Overview==
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The cI protein of bacteriophage lambda (lambdacI) activates transcription, by binding a DNA operator just upstream of the promoter and interacting, with the RNA polymerase sigma subunit domain 4 (sigma(4)). We determined, the crystal structure of the lambdacI/sigma(4)/DNA ternary complex at 2.3, A resolution. There are no conformational changes in either protein, which, interact through an extremely small interface involving at most 6 amino, acid residues. The interactions of the two proteins stabilize the binding, of each protein to the DNA. The results provide insight into how, activators can operate through a simple cooperative binding mechanism but, affect different steps of the transcription initiation process.
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The cI protein of bacteriophage lambda (lambdacI) activates transcription by binding a DNA operator just upstream of the promoter and interacting with the RNA polymerase sigma subunit domain 4 (sigma(4)). We determined the crystal structure of the lambdacI/sigma(4)/DNA ternary complex at 2.3 A resolution. There are no conformational changes in either protein, which interact through an extremely small interface involving at most 6 amino acid residues. The interactions of the two proteins stabilize the binding of each protein to the DNA. The results provide insight into how activators can operate through a simple cooperative binding mechanism but affect different steps of the transcription initiation process.
==About this Structure==
==About this Structure==
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1RIO is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Enterobacteria_phage_lambda Enterobacteria phage lambda] and [http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus] with CA and MPD as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RIO OCA].
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1RIO is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Enterobacteria_phage_lambda Enterobacteria phage lambda] and [http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=MPD:'>MPD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RIO OCA].
==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Thermus aquaticus]]
[[Category: Thermus aquaticus]]
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[[Category: Darst, S.A.]]
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[[Category: Darst, S A.]]
[[Category: Hochschild, A.]]
[[Category: Hochschild, A.]]
[[Category: Jain, D.]]
[[Category: Jain, D.]]
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[[Category: Nickels, B.E.]]
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[[Category: Nickels, B E.]]
[[Category: Sun, L.]]
[[Category: Sun, L.]]
[[Category: CA]]
[[Category: CA]]
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[[Category: transcription activation]]
[[Category: transcription activation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:37:40 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:51:17 2008''

Revision as of 12:51, 21 February 2008


1rio, resolution 2.30Å

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Structure of bacteriophage lambda cI-NTD in complex with sigma-region4 of Thermus aquaticus bound to DNA

Overview

The cI protein of bacteriophage lambda (lambdacI) activates transcription by binding a DNA operator just upstream of the promoter and interacting with the RNA polymerase sigma subunit domain 4 (sigma(4)). We determined the crystal structure of the lambdacI/sigma(4)/DNA ternary complex at 2.3 A resolution. There are no conformational changes in either protein, which interact through an extremely small interface involving at most 6 amino acid residues. The interactions of the two proteins stabilize the binding of each protein to the DNA. The results provide insight into how activators can operate through a simple cooperative binding mechanism but affect different steps of the transcription initiation process.

About this Structure

1RIO is a Protein complex structure of sequences from Enterobacteria phage lambda and Thermus aquaticus with and as ligands. Full crystallographic information is available from OCA.

Reference

Structure of a ternary transcription activation complex., Jain D, Nickels BE, Sun L, Hochschild A, Darst SA, Mol Cell. 2004 Jan 16;13(1):45-53. PMID:14731393

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