Structural analysis of the domain interface in DrrB, a response regulator of the OmpR/PhoB subfamily.

ABSTRACT: The N-terminal regulatory domains of bacterial response regulator proteins catalyze phosphoryl transfer and function as phosphorylation-dependent regulatory switches to control the output activities of C-terminal effector domains. Structures of numerous isolated regulatory and effector domains have been determined. However, a detailed understanding of regulatory interactions among these domains has been limited by the relative paucity of structural data for intact multidomain response regulator proteins. The first multidomain structures determined, those of transcription factor NarL and methylesterase CheB, both revealed extensive interdomain interfaces. The regulatory domains obstruct access to the functional sites of the effector domains, indicating a regulatory mechanism based on inhibi

SUBMITTER: Robinson VL 

PROVIDER: S-EPMC164896 | biostudies-literature | 2003 Jul

REPOSITORIES: biostudies-literature