Human CTP synthase filament structure reveals the active enzyme conformation

Volume: 24, Issue: 6, Pages: 507 - 514
Published: May 1, 2017
Abstract
The universally conserved enzyme CTP synthase (CTPS) forms filaments in bacteria and eukaryotes. In bacteria, polymerization inhibits CTPS activity and is required for nucleotide homeostasis. Here we show that for human CTPS, polymerization increases catalytic activity. The cryo-EM structures of bacterial and human CTPS filaments differ considerably in overall architecture and in the conformation of the CTPS protomer, explaining the divergent...
Paper Details
Title
Human CTP synthase filament structure reveals the active enzyme conformation
Published Date
May 1, 2017
Volume
24
Issue
6
Pages
507 - 514
Citation AnalysisPro
  • Scinapse’s Top 10 Citation Journals & Affiliations graph reveals the quality and authenticity of citations received by a paper.
  • Discover whether citations have been inflated due to self-citations, or if citations include institutional bias.