Ontology highlight
ABSTRACT:
SUBMITTER: Trempe JF
PROVIDER: S-EPMC3081552 | biostudies-literature | 2011 Apr
REPOSITORIES: biostudies-literature
Trempe Jean-François JF Shenker Solomon S Kozlov Guennadi G Gehring Kalle K
Protein science : a publication of the Protein Society 20110311 4
The N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a key bifunctional enzyme in the biosynthesis of UDP-GlcNAc, a precursor in the synthesis of cell wall peptidoglycan. Crystal structures of the enzyme from different bacterial strains showed that the polypeptide forms a trimer through a unique parallel left-handed beta helix domain. Here, we show that the GlmU enzyme from Escherichia coli forms a hexamer in solution. Sedimentation equilibrium analytical ultracentrifugation demonstra ...[more]