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The biotin repressor: thermodynamic coupling of corepressor binding, protein assembly, and sequence-specific DNA binding.
The Escherichia coli biotin repressor, an allosteric transcriptional regulator, is activated for binding to the biotin operator by the small molecule biotinyl-5'-AMP. Results of combinedExpand
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Multiple disordered loops function in corepressor-induced dimerization of the biotin repressor.
Cooperative association of the Escherichia coli biotin repressor with the biotin operator is allosterically activated by binding of the corepressor, bio-5'-AMP. The corepressor function of theExpand
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Coupling of protein assembly and DNA binding: biotin repressor dimerization precedes biotin operator binding.
The kinetics of coupling of protein dimerization and DNA binding have been investigated in the biotin repressor system. Two repressor monomers bind to the 40 base-pair biotin operator sequence. InExpand
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Ligand-linked structural changes in the Escherichia coli biotin repressor: the significance of surface loops for binding and allostery.
The Escherichia coli repressor of biotin biosynthesis (BirA) is an allosteric site-specific DNA-binding protein. BirA catalyzes synthesis of biotinyl-5'-AMP from substrates biotin and ATP and theExpand
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Binding specificity and the ligand dissociation process in the E. coli biotin holoenzyme synthetase
The binding of the Escherichia coli biotin holoenzyme synthetase to the two ligands, biotin and bio‐5′‐AMP, is coupled to disorder‐to‐order transitions in the protein. In the structure of the biotinExpand
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A map of the biotin repressor-biotin operator interface: binding of a winged helix-turn-helix protein dimer to a forty base-pair site.
The Escherichia coli biotin repressor is a member of the "winged helix-turn-helix" class of site-specific DNA binding proteins. The protein binds as a dimer to the 40 bp biotin operator sequence.Expand
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Nonenzymatic biotinylation of a biotin carboxyl carrier protein: Unusual reactivity of the physiological target lysine
Enzyme‐catalyzed addition of biotin to proteins is highly specific. In any single organism one or a small number of proteins are biotinylated and only a single lysine on each of these proteins isExpand
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Coupling of site-specific DNA binding to protein dimerization in assembly of the biotin repressor-biotin operator complex.
The Escherichia coli repressor of biotin biosynthesis, BirA, binds site-specifically to the biotin operator, a 40 base pair imperfect inverted palindrome. Two repressor monomers have been shown toExpand
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Allosteric signaling in the biotin repressor occurs via local folding coupled to global dampening of protein dynamics.
The biotin repressor is an allosterically regulated, site-specific DNA-binding protein. Binding of the small ligand bio-5'-AMP activates repressor dimerization, which is a prerequisite to DNAExpand
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The biotin regulatory system: kinetic control of a transcriptional switch.
An organism's response to environmental and metabolic cues requires communication between transcription regulatory processes and "other" cellular events. In a number of biological control circuits,Expand
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