Binding specificity and the ligand dissociation process in the E. coli biotin holoenzyme synthetase

Protein Science

Volumn 11, Issue 3, 2002, Pages 558-570

  Kwon, Keehwan ^a   Streaker, Emily D ^a   Beckett, Dorothy ^a  

^a Bldg 142   (United States)

Author keywords

Disorder to order transition; Ligand dissociation kinetics; Thermodynamics of ligand binding

Indexed keywords

ADENOSINE PHOSPHATE; APOENZYME; BIOTIN; BIOTIN SYNTHASE; GLYCINE; HOLOENZYME;

ARTICLE; BINDING AFFINITY; BINDING KINETICS; CALORIMETRY; CHEMICAL BOND; CONTROLLED STUDY; DISSOCIATION; ENERGY; ESCHERICHIA COLI; LIGAND BINDING; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; TEMPERATURE DEPENDENCE; THERMODYNAMICS;

ADENOSINE MONOPHOSPHATE; AMINO ACID SUBSTITUTION; BACTERIAL PROTEINS; BIOTIN; CARBON-NITROGEN LIGASES; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; KINETICS; LIGANDS; MUTATION; PROTEIN BINDING; REPRESSOR PROTEINS; THERMODYNAMICS; TRANSCRIPTION FACTORS;

ESCHERICHIA COLI; NEGIBACTERIA;

EID: 0036176908     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.33502     Document Type: Article

References (26)

1. Cooperative binding of the Escherichia coli repressor of biotin biosynthesis to the biotin operator
2. Evaluation of linked protonation effects in protein binding reactions using isothermal titration calorimetry
3. The birA gene of Escherichia coli encodes a biotin holoenzyme synthetase
4. Genetic and biochemical characterization of the birA gene and its product: Evidence for a direct role of biotin holoenzyme synthetase in repression of the biotin operon in Escherichia coli
5. Calorimetric investigation of proton linkage by monitoring both the enthalpy and association constant of binding: Application to the interaction of the Src SH2 domain with a highaffinity tyrosyl phosphopeptide
6. Thermodynamic and structural consequences of flexible loop deletion by circular permutation in the streptavidin-biotin system
7. Dimerization of the Escherichia coli biotin repressor: Corepressor function in protein assembly
8. Structural studies of the streptavidin binding loop
9. A structural snapshot of an intermediate on the streptavidin-biotin dissociation pathway
10. Calculation of protein extinction coefficients from amino acid sequence
11. Ser45 plays an important role in managing both the equilibrium and transition state energetics of the streptavidin-biotin system
12. Thermodynamics of ferredoxin binding to ferredoxin:NADP+ reductase and the role of water at the complex interface
13. MOLMOL: A program for display and analysis of macromolecular structures
14. Function of a conserved sequence motif in biotin holoenzyme synthetases
15. Multiple disordered loops function in corepressor-induced dimerization of the biotin repressor
16. The enzymatic synthesis of holotranscarboxylase from apotranscarboxylase and (+) biotin: II. Investigation of the reaction mechanism
17. Mutations of an epitope hot-spot residue alter rate-limiting steps of antigen-antibody protein-protein associations
18. Rates of ligand binding to periplasmic proteins involved in bacterial transport and chemotaxis
19. Streptavidin-biotin binding energetics
20. Evidence for multiple forms of biotin holocarboxylase synthetase in pea (pisum sativum) and in Arabidopsis thaliana: Subcellular fractionation studies and isolation of a cDNA clone
21. Corepressorinduced organization and assembly of the biotin repressor: A model for allosteric activation of a transcriptional regulator
22. Competing protein:protein interactions are proposed to control the biological switch of the E. coli biotin repressor
23. Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates biotin- and DNA-binding domains
24. Kinetics of biotinyl-5′-adenylate synthesis catalyzed by the Escher ichia coli repressor of biotin biosynthesis and the stability of the enzyme-product complex
25. Evidence for distinct ligand-bound conformational states of the multifunctional Escherichia coli repressor of biotin biosynthesis
26. Thermodynamic analysis of small ligand binding to the Escherichia coli repressor of biotin biosynthesis