Architecture of the soluble receptor Aer2 indicates an in-line mechanism for PAS and HAMP domain signaling.

ABSTRACT: Bacterial receptors typically contain modular architectures with distinct functional domains that combine to send signals in response to stimuli. Although the properties of individual components have been investigated in many contexts, there is little information about how diverse sets of modules work together in full-length receptors. Here, we investigate the architecture of Aer2, a soluble gas-sensing receptor that has emerged as a model for PAS (Per-Arnt-Sim) and poly-HAMP (histidine kinase-adenylyl cyclase-methyl-accepting chemotaxis protein-phosphatase) domain signaling. The crystal structure of the heme-binding PAS domain in the ferric, ligand-free form, in comparison to the previously determined cyanide-bound state, identifies conformational changes induced by ligand binding that ar

SUBMITTER: Airola MV 

PROVIDER: S-EPMC3577987 | biostudies-literature | 2013 Mar

REPOSITORIES: biostudies-literature