Ontology highlight
ABSTRACT:
SUBMITTER: Lynch EM
PROVIDER: S-EPMC5472220 | biostudies-literature | 2017 Jun
REPOSITORIES: biostudies-literature
Lynch Eric M EM Hicks Derrick R DR Shepherd Matthew M Endrizzi James A JA Maker Allison A Hansen Jesse M JM Barry Rachael M RM Gitai Zemer Z Baldwin Enoch P EP Kollman Justin M JM
Nature structural & molecular biology 20170501 6
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 consequences of polymerization on activity. The struc ...[more]