Ontology highlight
ABSTRACT:
SUBMITTER: Barry RM
PROVIDER: S-EPMC4126345 | biostudies-literature | 2014 Jul
REPOSITORIES: biostudies-literature
Barry Rachael M RM Bitbol Anne-Florence AF Lorestani Alexander A Charles Emeric J EJ Habrian Chris H CH Hansen Jesse M JM Li Hsin-Jung HJ Baldwin Enoch P EP Wingreen Ned S NS Kollman Justin M JM Gitai Zemer Z
eLife 20140716
CTP Synthetase (CtpS) is a universally conserved and essential metabolic enzyme. While many enzymes form small oligomers, CtpS forms large-scale filamentous structures of unknown function in prokaryotes and eukaryotes. By simultaneously monitoring CtpS polymerization and enzymatic activity, we show that polymerization inhibits activity, and CtpS's product, CTP, induces assembly. To understand how assembly inhibits activity, we used electron microscopy to define the structure of CtpS polymers. Th ...[more]