Thermodynamic and structural investigation of bispecificity in protein-protein interactions.

ABSTRACT: The ability of a single protein to interact with multiple protein partners is central to many biological processes. However, the physical-chemical and structural basis of the multispecificity is not understood. In Escherichia coli, the protein BirA can self-associate to a homodimer or form a heterodimer with the biotin carboxyl carrier protein of the biotin-dependent carboxylase, acetyl coenzyme A carboxylase. The first interaction results in binding of BirA to the biotin operator sequence to repress transcription initiation at the biotin biosynthetic operon and the second is a prerequisite to posttranslational biotin addition to the carrier protein for use in metabolism. A single surface on BirA is used for both interactions and previous studies indicate that, despite the structural diffe

SUBMITTER: Zhao H 

PROVIDER: S-EPMC2792886 | biostudies-literature | 2009 Jun

REPOSITORIES: biostudies-literature