Dataset Information
Micrographs for EMD-45746, EMD-45645, EMD-45646, and EMD-45665: Structure of WT DosP bound to c-di-GMP
Ontology highlight
ABSTRACT:
SUBMITTER: Daniel L Kober
PROVIDER: EMPIAR-12202 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Structures of the multi-domain oxygen sensor DosP: remote control of a c-di-GMP phosphodiesterase by a regulatory PAS domain.
Nature communications 20241107 1
The heme-based direct oxygen sensor DosP degrades c-di-GMP, a second messenger nearly unique to bacteria. In stationary phase Escherichia coli, DosP is the most abundant c-di-GMP phosphodiesterase. Ligation of O<sub>2</sub> to a heme-binding PAS domain (hPAS) of the protein enhances the phosphodiesterase through an allosteric mechanism that has remained elusive. We determine six structures of full-length DosP in its aerobic or anaerobic conformations, with or without c-di-GMP. DosP is an elongat ...[more]
