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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
1994-6-9
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pubmed:abstractText |
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.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Apoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Trp aporepressor protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/Tryptophan,
http://linkedlifedata.com/resource/pubmed/chemical/tryptophan repressor protein
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0022-2836
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
13
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pubmed:volume |
238
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
592-614
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:8176748-Amino Acid Sequence,
pubmed-meshheading:8176748-Apoproteins,
pubmed-meshheading:8176748-Bacterial Proteins,
pubmed-meshheading:8176748-Base Sequence,
pubmed-meshheading:8176748-DNA, Bacterial,
pubmed-meshheading:8176748-Escherichia coli Proteins,
pubmed-meshheading:8176748-Hydrogen Bonding,
pubmed-meshheading:8176748-Magnetic Resonance Spectroscopy,
pubmed-meshheading:8176748-Models, Molecular,
pubmed-meshheading:8176748-Molecular Sequence Data,
pubmed-meshheading:8176748-Operator Regions, Genetic,
pubmed-meshheading:8176748-Osmolar Concentration,
pubmed-meshheading:8176748-Protein Binding,
pubmed-meshheading:8176748-Protein Structure, Secondary,
pubmed-meshheading:8176748-Repressor Proteins,
pubmed-meshheading:8176748-Tryptophan
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pubmed:year |
1994
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pubmed:articleTitle |
The solution structures of the trp repressor-operator DNA complex.
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pubmed:affiliation |
Stanford Magnetic Resonance Laboratory, CA 94305-5055.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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