The Lac repressor: A second generation of structural and functional studies

Current Opinion in Structural Biology

Volumn 11, Issue 1, 2001, Pages 19-25

  Bell, C E ^a   Lewis, M ^a  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ISOPROPYL BETA THIOGALACTOSIDE; LAC REPRESSOR PROTEIN; REPRESSOR PROTEIN; THIOGLYCOSIDE; UNCLASSIFIED DRUG;

ALLOSTERISM; BINDING SITE; CRYSTAL STRUCTURE; DNA BINDING; DNA SEQUENCE; GENE CONTROL; OPERATOR GENE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DNA BINDING; PROTEIN DNA INTERACTION; PROTEIN STRUCTURE; REVIEW; SEQUENCE ANALYSIS;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA;

EID: 0035253082     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(00)00180-9     Document Type: Review

References (27)

1. Lactose repressor protein: Functional properties and structure
2. Crystal structure of Lac repressor core tetramer and its implications for DNA looping
3. Crystal structure of the lactose operon repressor and its complexes with DNA and inducer
4. Structure of the complex of Lac repressor headpiece and an 11 base-pair half-operator determined by nuclear magnetic resonance spectroscopy and restrained molecular dynamics
5. Refined structure of lac repressor headpiece (1-56) determined by relaxation matrix calculations from 2D and 3D NOE data: Change of tertiary structure upon binding to lac operator
6. Formation of the hinge helix in the lac repressor is induced upon binding to the lac operator
7. 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
8. Lac repressor genetic map in real space
9. Designed disulfide between N-terminal domains of lactose repressor disrupts allosteric linkage
10. A closer view of the conformation of the Lac repressor bound to operator
11. Lac repressor-operator interaction. II. Effect of galactosides and other ligands
12. Crystal structure of LacI member, PurR, bound to DNA: Minor groove binding by alpha helices
13. Escherichia coli purine repressor: Key residues for the allosteric transition between active and inactive conformations and for interdomain signaling
14. Glycine insertion in the hinge region of lactose repressor protein alters DNA binding
15. Substitutions at histidine 74 and aspartate 278 alter ligand binding and allostery in lactose repressor protein
16. Dimerisation mutants of Lac repressor. II. A single amino acid substitution, D278L, changes the specificity of dimerisation
17. Dimerisation mutants of Lac repressor. I. A monomeric mutant, L251A, that binds lac operator DNA as a dimer
18. Strengthening the dimerisation interface of Lac repressor increases its thermostability by 40°C
19. Thermodynamic analysis of unfolding and dissociation in lactose repressor protein
20. Combinatorial mutations of the lac repressor: Stability of the monomer-monomer interface is increased by apolar substitution at position 84
21. The solution structure of Lac repressor headpiece 62 complexed to a symmetrical lac operator
22. A perfectly symmetric lac operator binds the Lac repressor very tightly
23. The locus of sequence-directed and protein-induced DNA bending
24. DNA bend direction by phase sensitive detection
25. DNA bending by negative regulatory proteins: Gal and Lac repressors
26. Hinge-helix formation and DNA bending in various Lac repressor-operator complexes
27. Operator DNA sequence variation enhances high affinity binding by hinge helix mutants of lactose repressor protein