Abstract
Publisher Summary This chapter describes Escherichia coli ( E. Coli ) repressor of biotin biosynthesis. The repressor of biotin biosynthesis is an allosteric site-specific DNA-binding protein that also catalyzes an essential posttranslational modification reaction. Results of the studies described in the chapter reveal structural and thermodynamic details of BirA function. These results, moreover, serve to direct the course of future studies of the protein. An elucidation of the structural details of regulation of BirA function via small ligand binding requires high-resolution structures of complexes of the protein bound to biotin and bio-5'-AMP. A high-resolution structure of the ternary holoBirA–bioO complex reveals how a dimeric helix-turn-helix protein interacts with an unusually large 40-bp target site. Thermodynamic and kinetic studies of the multiple macromolecular interactions in which BirA participates provide information critical to a complete understanding of the functional energetics of this unique regulatory protein.
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