From Proteopedia
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| - | [[Image:1cjg.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1cjg| PDB=1cjg | SCENE= }} | | {{STRUCTURE_1cjg| PDB=1cjg | SCENE= }} |
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| - | '''NMR STRUCTURE OF LAC REPRESSOR HP62-DNA COMPLEX'''
| + | ===NMR STRUCTURE OF LAC REPRESSOR HP62-DNA COMPLEX=== |
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| - | ==Overview==
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| - | BACKGROUND: Lactose repressor protein (Lac) controls the expression of the lactose metabolic genes in Escherichia coli by binding to an operator sequence in the promoter of the lac operon. Binding of inducer molecules to the Lac core domain induces changes in tertiary structure that are propagated to the DNA-binding domain through the connecting hinge region, thereby reducing the affinity for the operator. Protein-protein and protein-DNA interactions involving the hinge region play a crucial role in the allosteric changes occurring upon induction, but have not, as yet, been analyzed in atomic detail. RESULTS: We have used nuclear magnetic resonance (NMR) spectroscopy and restrained molecular dynamics (rMD) to determine the structure of the Lac repressor DNA-binding domain (headpeice 62; HP62) in complex with a symmetrized lac operator. Analysis of the structures reveals specific interactions between Lac repressor and DNA that were not found in previously investigated Lac repressor-DNA complexes. Important differences with the previously reported structures of the HP56-DNA complex were found in the loop following the helix-turn-helix (HTH) motif. The protein-protein and protein-DNA interactions involving the hinge region and the deformations in the DNA structure could be delineated in atomic detail. The structures were also used for comparison with the available crystallographic data on the Lac and Pur repressor-DNA complexes. CONCLUSIONS: The structures of the HP62-DNA complex provide the basis for a better understanding of the specific recognition in the Lac repressor-operator complex. In addition, the structural features of the hinge region provide detailed insight into the protein-protein and protein-DNA interactions responsible for the high affinity of the repressor for operator DNA.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_10647179}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 10647179 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_10647179}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 1CJG 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=1CJG OCA]. | + | 1CJG is a [[Single protein]] structure of 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=1CJG OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Lac repressor]] | | [[Category: Lac repressor]] |
| | [[Category: Transcription regulation]] | | [[Category: Transcription regulation]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:48:09 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:50:06 2008'' |
Revision as of 17:50, 30 June 2008
Template:STRUCTURE 1cjg
NMR STRUCTURE OF LAC REPRESSOR HP62-DNA COMPLEX
Template:ABSTRACT PUBMED 10647179
About this Structure
1CJG is a Single protein structure of sequence from Escherichia coli. Full experimental information is available from OCA.
Reference
The solution structure of Lac repressor headpiece 62 complexed to a symmetrical lac operator., Spronk CA, Bonvin AM, Radha PK, Melacini G, Boelens R, Kaptein R, Structure. 1999 Dec 15;7(12):1483-92. PMID:10647179
Page seeded by OCA on Mon Jun 30 20:50:06 2008
