Crystal structures of adenylylated and unadenylylated P_II protein GlnK from Corynebacterium glutamicum.

ABSTRACT: P_II proteins are ubiquitous signaling proteins that are involved in the regulation of the nitrogen/carbon balance in bacteria, archaea, and some plants and algae. Signal transduction via P_II proteins is modulated by effector molecules and post-translational modifications in the P_II T-loop. Whereas the binding of ADP, ATP and the concomitant binding of ATP and 2-oxoglutarate (2OG) engender two distinct conformations of the T-loop that either favor or disfavor the interaction with partner proteins, the structural consequences of post-translational modifications such as phosphorylation, uridylylation and adenylylation are far less well understood. In the present study, crystal structures of the P_II protein GlnK from Corynebacterium glutamicum have b

SUBMITTER: Grau FC 

PROVIDER: S-EPMC7919409 | biostudies-literature | 2021 Mar

REPOSITORIES: biostudies-literature