PMID: 7011373Feb 17, 1981Paper

High-resolution nuclear magnetic resonance studies of the Lac repressor. 1. Assignments of tyrosine resonances in the N-terminal headpiece

Biochemistry
A A RibeiroO Jardetzky

Abstract

The DNA binding site of the lac repressor protein has been implicated to lie within the N-terminal 51 amino acid fragment termed headpiece (HP-51 or LR-51). High-resolution NMR suggests that isolated HP-51 retains most of the secondary and tertiary structure which it has in the whole repressor. Four of the eight tyrosines of repressor are in HP-51. 1H NMR spectra (360 MHz) over the aromatic region of native HP-51 show that the four tyrosines are nonequivalent with an unusual distribution of chemical shifts. Denaturation leads to loss of these chemical shift differences. Homonuclear decoupling and a two-dimensional autocorrelated spectrum allow unequivocal pairing of resonances from Tyr A at 6.99 and 6.79 ppm, Tyr B at 6.98 and 6.39 ppm, Tyr C at 6.70 and 6.54 ppm, and Tyr D at 6.39 and 6.33 ppm. The 2,6 protons are low field of the 3,5 protons for each Tyr residue. Selective chemical modification with nitration reagents allows assignments of Tyr A to Tyr-47, Tyr B to Tyr-7, Tyr C to Tyr-12, and Tyr D to Tyr-17 in HP-51. All four tyrosines are essential for maintaining the structure of the isolated headpiece, and Tyr-7, -12, and -17 appear to be stacked.

References

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Citations

Nov 9, 1981·Biochimica Et Biophysica Acta·J K Roberts, O Jardetzky
Jan 1, 1982·Proceedings of the National Academy of Sciences of the United States of America·H NickP Lu
Mar 1, 1982·Proceedings of the National Academy of Sciences of the United States of America·B W MatthewsY Takeda
Oct 1, 1983·Proceedings of the National Academy of Sciences of the United States of America·E R ZuiderwegK Wüthrich
May 2, 1983·European Journal of Biochemistry·F BuckW E Hull
Feb 2, 2013·Biochemistry·Paul J BarrettCharles R Sanders
Apr 3, 1982·Biochimica Et Biophysica Acta·M Schnarr, J C Maurizot
Jun 29, 1981·FEBS Letters·D M ParkerG C Roberts

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