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| ==NMR STUDY OF TRP REPRESSOR-OPERATOR DNA COMPLEX== | | ==NMR STUDY OF TRP REPRESSOR-OPERATOR DNA COMPLEX== |
- | <StructureSection load='1rcs' size='340' side='right' caption='[[1rcs]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''> | + | <StructureSection load='1rcs' size='340' side='right'caption='[[1rcs]]' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[1rcs]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RCS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RCS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1rcs]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RCS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RCS FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rcs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rcs OCA], [http://pdbe.org/1rcs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rcs RCSB], [http://www.ebi.ac.uk/pdbsum/1rcs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1rcs ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</scene></td></tr> |
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1rcs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rcs OCA], [https://pdbe.org/1rcs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rcs RCSB], [https://www.ebi.ac.uk/pdbsum/1rcs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rcs ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://www.uniprot.org/uniprot/TRPR_ECOLI TRPR_ECOLI]] This protein is an aporepressor. When complexed with L-tryptophan it binds the operator region of the trp operon (5'-ACTAGT-'3') and prevents the initiation of transcription. The complex also regulates trp repressor biosynthesis by binding to its regulatory region. | + | [https://www.uniprot.org/uniprot/TRPR_ECOLI TRPR_ECOLI] This protein is an aporepressor. When complexed with L-tryptophan it binds the operator region of the trp operon (5'-ACTAGT-'3') and prevents the initiation of transcription. The complex also regulates trp repressor biosynthesis by binding to its regulatory region. |
| == Evolutionary Conservation == | | == Evolutionary Conservation == |
| [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| </StructureSection> | | </StructureSection> |
| [[Category: Escherichia coli]] | | [[Category: Escherichia coli]] |
- | [[Category: Zhao, D]] | + | [[Category: Large Structures]] |
- | [[Category: Zheng, Z]] | + | [[Category: Zhao D]] |
- | [[Category: Dna]] | + | [[Category: Zheng Z]] |
- | [[Category: Dna-binding]]
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- | [[Category: Repressor]]
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- | [[Category: Transcription regulation]]
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- | [[Category: Transcription-dna complex]]
| + | |
- | [[Category: Trp]]
| + | |
| Structural highlights
Function
TRPR_ECOLI This protein is an aporepressor. When complexed with L-tryptophan it binds the operator region of the trp operon (5'-ACTAGT-'3') and prevents the initiation of transcription. The complex also regulates trp repressor biosynthesis by binding to its regulatory region.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zhang H, Zhao D, Revington M, Lee W, Jia X, Arrowsmith C, Jardetzky O. The solution structures of the trp repressor-operator DNA complex. J Mol Biol. 1994 May 13;238(4):592-614. PMID:8176748 doi:http://dx.doi.org/10.1006/jmbi.1994.1317
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