Structural Analysis of Lac Repressor Bound to Allosteric Effectors

Journal of Molecular Biology

Volumn 370, Issue 4, 2007, Pages 609-619

  Daber, Robert ^a   Stayrook, Steven ^a   Rosenberg, Allison ^a   Lewis, Mitchell ^a  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

allostery; conformational change; effector binding; inducer; Lac repressor

Indexed keywords

HYDROXYL GROUP; LAC PROTEIN; REPRESSOR PROTEIN; UNCLASSIFIED DRUG; WATER;

ALLOSTERISM; AMINO TERMINAL SEQUENCE; ARTICLE; BINDING KINETICS; CARBOXY TERMINAL SEQUENCE; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; GENE INDUCTION; GENE STRUCTURE; HYDROGEN BOND; MOLECULAR DYNAMICS; OPERON; PRIORITY JOURNAL; PROTEIN CONFORMATION; STRUCTURE ANALYSIS;

EID: 34249951731     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.04.028     Document Type: Article

References (27)

1. Jacob F., and Monod J. Genetic regulatory mechanisms in the synthesis of proteins. J. Mol. Biol. 3 (1961) 318-356
2. Friedman A.M., Fischmann T.O., and Steitz T.A. Crystal structure of lac repressor core tetramer and its implications for DNA looping. Science 268 (1995) 1721-1727
3. Lewis M., Chang G., Horton N.C., Kercher M.A., Pace H.C., Schumacher M.A., et al. Crystal structure of the lactose operon repressor and its complexes with DNA and inducer. [see comment]. Science 271 (1996) 1247-1254
4. Wade-Jardetzky N., Bray R.P., Conover W.W., Jardetzky O., Geisler N., and Weber K. Differential mobility of the N-terminal headpiece in the lac-repressor protein. J. Mol. Biol. 128 (1979) 259-264
5. Gilbert W., and Maxam A. The nucleotide sequence of the lac operator. Proc. Natl Acad. Sci. USA 70 (1973) 3581-3584
6. Jobe A., and Bourgeois S. lac Repressor-operator interaction. VI. The natural inducer of the lac operon. Journal of Molecular Biology 69 (1972) 397-408
7. Monod J., Cohen-Bazire G., and Cohn M. Biochim. Biophys. Acta 7 (1951) 585
8. Muller-Hill B., Rickenberg H.V., and Wallenfels K. Specificity of th Induction of the Enzymes of the Lac Operon in Escherichia coli. J. Molec. Biol. 10 (1964) 303-318
9. Jobe A., and Bourgeois S. Lac repressor-operator interaction. VIII. Lactose is an anti-inducer of the lac operon. J. Molec. Biol. 75 (1973) 303-313
10. Jarrett H.W. Temperature dependence of DNA affinity chromatography of transcription factors. Analytical Biochemistry 279 (2000) 209-217
11. Riggs A.D., Newby R.F., and Bourgeois S. lac Repressor-Operator Interaction II. Effect of galactosides and other ligands. J. Mol. Biol. 51 (1970) 303-314
12. Barkley M.D., Riggs A.D., Jobe A., and Burgeois S. Interaction of effecting ligands with lac repressor and repressor-operator complex. Biochemistry 14 (1975) 1700-1712
13. Bell C.E., and Lewis M. The Lac repressor: a second generation of structural and functional studies. Current Opinion in Structural Biology 11 (2001) 19-25
14. Bell C.E., Barry J., Matthews K.S., and Lewis M. Structure of a variant of lac repressor with increased thermostability and decreased affinity for operator. Journal of Molecular Biology 313 (2001) 99-109
15. Bell C.E., and Lewis M. A closer view of the conformation of the Lac repressor bound to operator. Nature Structural Biology 7 (2000) 209-214
16. Laiken S.L., Gross C.A., and Von Hippel P.H. Equilibrium and kinetic studies of Escherichia coli lac repressor-inducer interactions. Journal of Molecular Biology 66 (1972) 143-155
17. Oshima Y., Matsuura M., and Horiuchi T. Conformational change of the lac repressor induced with the inducer. Biochemical and Biophysical Research Communications 47 (1972) 1444-1450
18. Matthews H.R., Thielmann H.W., Matthews K.S., and Jardetzky O. NMR studies of the binding of an inducer and an anti-inducer to the lac repressor. Annals of the New York Academy of Sciences 222 (1973) 226-229
19. Markiewicz P., Kleina L.G., Cruz C., Ehret S., and Miller J.H. Genetic studies of the lac repressor. XIV. Analysis of 4000 altered Escherichia coli lac repressors reveals essential and non-essential residues, as well as "spacers" which do not require a specific sequence. Journal of Molecular Biology 240 (1994) 421-433
20. Pace H.C., Kercher M.A., Lu P., Markiewicz P., Miller J.H., Chang G., and Lewis M. Lac repressor genetic map in real space. Trends in Biochemical Sciences 22 (1997) 334-339
21. Flynn T.C., Swint-Kruse L., Kong Y., Booth C., Matthews K.S., and Ma J. Allosteric transition pathways in the lactose repressor protein core domains: asymmetric motions in a homodimer. Protein Science 12 (2003) 2523-2541
22. Montero E., Garcia-Herrero A., Asensio K.H., Ogawa J.S., Santoyo-Gonzalez F., Canada F., and Jimenez-Barbero J. The conformational behavior of non-hydrolyzable lactose analogues: the thioglycoside, carbaglycoside, and carba-iminoglycoside cases. Eur. J. Org. Chem. (2000) 1945-1952
23. Otwinowski Z., and Minor W. Processing of x-ray diffraction data collected in oscillation mode. Meth. Enzymol. 276 (1997) 307-326
24. Navaza J. AMoRe: an automated package for molecular replacement. Acta Cryst. D50 (1994) 157-163
25. Emsley P., and Cowtan K. Coot: model-building tools for molecular graphics. Acta crystallographica section D-biological crystallography 60 (2004) 2126-2132
26. Brunger A.T. Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355 (1992) 472-475
27. Kraulis P. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24 (1991) 946-950