1rcs

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[[Image:1rcs.gif|left|200px]]<br /><applet load="1rcs" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1rcs.gif|left|200px]]
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caption="1rcs" />
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'''NMR STUDY OF TRP REPRESSOR-OPERATOR DNA COMPLEX'''<br />
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{{Structure
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|PDB= 1rcs |SIZE=350|CAPTION= <scene name='initialview01'>1rcs</scene>
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|SITE=
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|LIGAND= <scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''NMR STUDY OF TRP REPRESSOR-OPERATOR DNA COMPLEX'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1RCS 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=TRP:'>TRP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RCS OCA].
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1RCS is a [[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=1RCS OCA].
==Reference==
==Reference==
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The solution structures of the trp repressor-operator DNA complex., Zhang H, Zhao D, Revington M, Lee W, Jia X, Arrowsmith C, Jardetzky O, J Mol Biol. 1994 May 13;238(4):592-614. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8176748 8176748]
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The solution structures of the trp repressor-operator DNA complex., Zhang H, Zhao D, Revington M, Lee W, Jia X, Arrowsmith C, Jardetzky O, J Mol Biol. 1994 May 13;238(4):592-614. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8176748 8176748]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: trp]]
[[Category: trp]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:49:32 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:49:49 2008''

Revision as of 11:49, 20 March 2008

Image:1rcs.gif


PDB ID 1rcs

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Ligands:
Coordinates: save as pdb, mmCIF, xml



NMR STUDY OF TRP REPRESSOR-OPERATOR DNA COMPLEX


Overview

The solution structures of the complex between Escherichia coli trp holorepressor and a 20 base-pair consensus operator DNA were determined. The majority of proton chemical shifts of the trp holorepressor and operator DNA were assigned from homonuclear 2D NOESY spectra of selectively deuterated analog-operator DNA complexes and the 3D NOESY-HMQC spectrum of a uniformly 15N-labeled repressor-operator DNA complex. The structures were calculated using restrained molecular dynamics and sequential simulated annealing with 4086 NOE and other experimental constraints. The root-mean-squared deviation (RMSD) among the calculated structures and their mean is 0.9(+/- 0.3)A for the repressor backbone, 1.1(+/- 0.5)A for the DNA backbone, and 1.3(+/- 0.3)A for all heavy atoms. The DNA is deformed to a significant extent from the standard B DNA structure to fit the helix-turn-helix (HTH) segment of the repressor (helices D and E) into its major grooves. Little change is found in the ABCF core of the repressor on complexation in comparison to the free repressor, but changes in the cofactor L-tryptophan binding pocket and the HTH segment are observed. The N-terminal residues (2 to 17) are found to be disordered and do not form stable interactions with DNA. Direct H-bonding to the bases of the operator DNA is consistent with all of our observed NOE constraints. Hydrogen bonds from NH eta 1 and NH eta 2 of Arg69 to O-6 and N-7 of G2 are compatible with the solution structure, as they are with the crystal structure. Other direct H-bonds from Lys72, Ala80, Ile79, Thr83 and Arg84 to base-pair functional groups can also be formed in our solution structures.

About this Structure

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

Reference

The solution structures of the trp repressor-operator DNA complex., Zhang H, Zhao D, Revington M, Lee W, Jia X, Arrowsmith C, Jardetzky O, J Mol Biol. 1994 May 13;238(4):592-614. PMID:8176748

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