Linked Life Data

12356295

Source:http://linkedlifedata.com/resource/pubmed/id/12356295

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
40
pubmed:dateCreated
2002-10-1
pubmed:abstractText
L75F-TrpR is a temperature-sensitive mutant of the tryptophan repressor protein of Escherichia coli in which surface-exposed residue leucine 75 in the DNA binding domain is replaced with phenylalanine. Biochemical and biophysical studies had suggested global alterations in dynamics for L75F-TrpR, although the structure was apparently similar to that of wild-type TrpR. Herein, we report the three-dimensional solution structure of apo-L75F-TrpR determined by multidimensional ((1)H, (15)N, and (13)C) solution NMR spectroscopy. An ensemble of structures was generated from 769 unique NOE-based distance restraints, 68 dihedral angle restraints, and 62 hydrogen bond distance restraints. Apo-L75F-TrpR exhibits a three-dimensional (3D) fold very similar to that of apo-WT-TrpR, with a dimeric core of four alpha-helices (A-C and F) from each subunit, and less well-defined D and E helical regions of the DNA binding domains. Despite their many similarities, wild-type and mutant proteins display significant chemical shift differences, one cluster of which is in the B-C turn, too distant to be ascribed solely to ring current effects from Phe75. Differences in NOE patterns and amide proton exchange rates are also observed in the B-C turn region. The data provide evidence that this point mutation exerts local effects on structure and stability in the DNA binding domain, and propagates long-range effects through the tertiary structure.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
8
pubmed:volume
41
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
11954-62
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Three-dimensional solution NMR structure of Apo-L75F-TrpR, a temperature-sensitive mutant of the tryptophan repressor protein.
pubmed:affiliation
Department of Chemistry and Biochemistry, Montana State University, 108 Gaines Hall, Bozeman, MT 59717, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.