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Journal of Bacteriology, July 2003, p. 4186-4194, Vol. 185, No. 14
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.14.4186-4194.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Structural Analysis of the Domain Interface in DrrB, a Response Regulator of the OmpR/PhoB Subfamily

Victoria L. Robinson, Ti Wu, and Ann M. Stock*

Howard Hughes Medical Institute, Center for Advanced Biotechnology and Medicine, and Department of Biochemistry, Robert Wood Johnson Medical School, The University of Medicine and Dentistry of New Jersey, Piscataway, New Jersey 08854

Received 6 March 2003/ Accepted 16 April 2003

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 inhibition. In contrast, the recently determined structure of the OmpR/PhoB homologue DrrD revealed no significant interdomain interface, suggesting that the domains are tethered by a flexible linker and lack a fixed orientation relative to each other. To address the generality of this feature, we have determined the 1.8-Å resolution crystal structure of Thermotoga maritima DrrB, providing a second structure of a multidomain response regulator of the OmpR/PhoB subfamily. The structure reveals an extensive domain interface of 751 Å2 and therefore differs greatly from that observed in DrrD. Residues that are crucial players in defining the activation state of the regulatory domain contribute to this interface, implying that conformational changes associated with phosphorylation will influence these intramolecular contacts. The DrrB and DrrD structures are suggestive of different signaling mechanisms, with intramolecular communication between N- and C-terminal domains making substantially different contributions to effector domain regulation in individual members of the OmpR/PhoB family.

* Corresponding author. Mailing address: CABM, 679 Hoes La., Piscataway, NJ 08854-5627. Phone: (732) 235-4844. Fax: (732) 235-5289. E-mail: stock{at}cabm.rutgers.edu.

Journal of Bacteriology, July 2003, p. 4186-4194, Vol. 185, No. 14
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.14.4186-4194.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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