By Yoko Eguchi, Ryutaro Utsumi (auth.), Ryutaro Utsumi PhD (eds.)
This interesting booklet encourages many microbiologists and scholars to go into the hot international of sign transduction in microbiology. over the last decade, an unlimited quantity of fascinating new details at the sign transduction pathway in micro organism has been dropped at mild. experiences on those advancements were prepare during this ebook, Bacterial sign Transduction: Networks and Drug pursuits. the purpose of this e-book is to supply an incentive for graduate scholars, educational scientists, and researchers within the pharmaceutical to extra elucidate the TCS networks and observe them within the look for novel drugs.
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Additional resources for Bacterial Signal Transduction: Networks and Drug Targets
PmrD binds to the phosphorylated form of the PmrA protein (green line), resulting in binding to the pbgP and ugd promoters and transcription of the pbgP and ugd genes. The phosphorylated PmrA protein represses transcription of the pmrD gene (red line). Fe3+ activates the PmrAlPmrB system directly. B) Model illustrating direct regulation of the pbgP and ugd genes where the PhoQ/PhoP system promotes transcription of the pbgP and ugd genes directly in response to low M g 2+ in Yersinia. Fe3+ activates the PmrB/PmrA system directly.
HK is a multi-domain protein composed ofsensor and histidine kinase domains (Fig. IA) and the histidine kinase domain is further divided into a dimerization and a catalytic domain. The structure and mechanism of histidine kinase domain of HK is highly conserved among TCS. In response to the sensing of an external stimuli or a ligand in the sensor domain, the special His residue in the dimerization domain is phosphorylated using ATP, which is catalyzed by the catalytic domain (autophosphorylation).
At the first stage of structural biology ofTCS, crystallographic and NMRanalyses ofdomain blocks revealed the folds and the remarkable regions ofsensor, dimerization and catalytic domains ofHK and receiver and effecter domains ofRR. As the second stage, the advanced researches oftheir multi-domain form and HK/RR complex showed the inter-domain and inter-molecular interactions and implied that the dynamic conformation changes are required in the signaling process. Thus, this chapter describes what these structural analyses ofTCS proteins have contributed in understanding the cell signaling mechanism; signal input -+ phosphoryl transfer -+ signal output.