Literature DB >> 3586020

Complex of lac repressor headpiece with a 14 base-pair lac operator fragment studied by two-dimensional nuclear magnetic resonance.

R Boelens, R M Scheek, J H van Boom, R Kaptein.   

Abstract

Two-dimensional nuclear Overhauser enhancement spectra are presented of the complex of lac repressor headpiece with a 14 base-pair lac operator fragment. Analysis of nuclear Overhauser enhancements observed between protein and DNA shows that the second helix of the headpiece ("the recognition helix") binds in the major groove of DNA as has been suggested, but that the orientation of this helix is approximately 180 degrees different from the proposed models.

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Year:  1987        PMID： 3586020     DOI： 10.1016/0022-2836(87)90638-3

Source DB:  PubMed          Journal:  J Mol Biol        ISSN： 0022-2836            Impact factor:   5.469


  21 in total

1.  Specificities of three tight-binding Lac repressors.

Authors:  P Kolkhof
Journal:  Nucleic Acids Res       Date:  1992-10-11       Impact factor: 16.971

2.  Contacts between Bacillus subtilis catabolite regulatory protein CcpA and amyO target site.

Authors:  J H Kim; G H Chambliss
Journal:  Nucleic Acids Res       Date:  1997-09-01       Impact factor: 16.971

3.  Orientation of the Lac repressor DNA binding domain in complex with the left lac operator half site characterized by affinity cleaving.

Authors:  J A Shin; R H Ebright; P B Dervan
Journal:  Nucleic Acids Res       Date:  1991-10-11       Impact factor: 16.971

4.  Protein-DNA conformational changes in the crystal structure of a lambda Cro-operator complex.

Authors:  R G Brennan; S L Roderick; Y Takeda; B W Matthews
Journal:  Proc Natl Acad Sci U S A       Date:  1990-10       Impact factor: 11.205

5.  Selectively 13C-enriched DNA: evidence from 13C1' relaxation rate measurements of an internal dynamics sequence effect in the lac operator.

Authors:  F Paquet; F Gaudin; G Lancelot
Journal:  J Biomol NMR       Date:  1996-10       Impact factor: 2.835

6.  The amino-terminal domain of LexA repressor is alpha-helical but differs from canonical helix-turn-helix proteins: a two-dimensional 1H NMR study.

Authors:  R M Lamerichs; A Padilla; R Boelens; R Kaptein; G Ottleben; H Rüterjans; M Granger-Schnarr; P Oertel; M Schnarr
Journal:  Proc Natl Acad Sci U S A       Date:  1989-09       Impact factor: 11.205

7.  NMR studies on protein-nucleic acid interaction.

Authors:  Robert Kaptein
Journal:  J Biomol NMR       Date:  2013-05       Impact factor: 2.835

8.  Recognition helices of lac and lambda repressor are oriented in opposite directions and recognize similar DNA sequences.

Authors:  N Lehming; J Sartorius; S Oehler; B von Wilcken-Bergmann; B Müller-Hill
Journal:  Proc Natl Acad Sci U S A       Date:  1988-11       Impact factor: 11.205

9.  Modified nucleotides reveal the indirect role of the central base pairs in stabilizing the lac repressor-operator complex.

Authors:  X Zhang; P A Gottlieb
Journal:  Nucleic Acids Res       Date:  1995-05-11       Impact factor: 16.971

10.  Photo-CIDNP study of the interaction between the glucocorticoid receptor DNA-binding domain and glucocorticoid response elements.

Authors:  E Kellenbach; T Härd; R Boelens; K Dahlman; J Carlstedt-Duke; J A Gustafsson; G A van der Marel; J H van Boom; B Maler; K R Yamamoto
Journal:  J Biomol NMR       Date:  1991-05       Impact factor: 2.835
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