Structural studies of the NOD module of the transcriptional activator MalT in complex with its regulatory proteins MalK, MalY, and Aes

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MalT is the global transcriptional activator of the maltose regulon in E. coli. It belongs to the newly recognized class of Signal Transduction ATPases with Numerous Domains (STAND), resembling a complex regulatory switch that responds to positive signals, such as ATP and maltotriose, as well as negative signals, mediated by the interaction with the cytoplasmic proteins MalK, MalY, and Aes. The structures of MalK, MalY and Aes have been determined, but their interaction site, the Nucleotide-binding-Oligomerization Domain (NOD) of MalT, as well as the molecular details of their interactions remain to be elucidated. We aim to provide structural and functional insights into the NOD module of MalT and its interactions with the negative effectors MalK, MalY, and Aes. To this end, different MalT fragments will be investigated for their ability to form complexes with MalK, MalY, or Aes. We will also attempt to co-crystallize the resulting complexes and to determine their X-ray structures. These studies are expected to provide a detailed structural view of the signaling processes involved in MalT regulation and will contribute to our understanding of the signaling by STAND proteins in general.