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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1993-3-16
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pubmed:abstractText |
The solution structures of the trp-repressor from Escherichia coli in both the liganded (holo-) and unliganded (apo-) form, have been refined by restrained molecular dynamics with simulated annealing using the program XPLOR and additional experimental constraints. The ensemble of refined holorepressor structures have a root-mean-square deviation (r.m.s.d.) of 0.8 A relative to the average structure for the backbone of the dimer core (helices A, B, C, A', B', C') and 2.5 A for the helix-turn-helix DNA-binding domain (helices D and E). The corresponding values for the aporepressor are 0.9 A for the backbone of the ABC-dimer core and 3.2 A for the DE helix-turn-helix. The r.m.s.d. of the average structures from the corresponding crystal structures are 2.3 A for the holorepressor ABC core and 4.2 A for its DE region; 2.3 A for the aporepressor core and 5.5 A for its DE region. The relative disorder of the DNA-binding domain is reflected in a number of experimental parameters including substantially more rapid backbone proton exchange rates, exchange-limited relaxation times and crystallographic B-factors. The stabilizing effect of the L-Trp ligand is evident in these measurements, as it is in the higher precision of the holorepressor structure.
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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/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Solutions,
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 |
Feb
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pubmed:issn |
0022-2836
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
229
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
735-46
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:8433368-Amino Acid Sequence,
pubmed-meshheading:8433368-Bacterial Proteins,
pubmed-meshheading:8433368-Computer Simulation,
pubmed-meshheading:8433368-Escherichia coli,
pubmed-meshheading:8433368-Magnetic Resonance Spectroscopy,
pubmed-meshheading:8433368-Molecular Sequence Data,
pubmed-meshheading:8433368-Protein Conformation,
pubmed-meshheading:8433368-Repressor Proteins,
pubmed-meshheading:8433368-Solutions,
pubmed-meshheading:8433368-Tryptophan
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pubmed:year |
1993
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pubmed:articleTitle |
Refined solution structures of the Escherichia coli trp holo- and aporepressor.
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pubmed:affiliation |
Stanford Magnetic Resonance Laboratory, Stanford University, CA 94305-5055.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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