PMID:21370307

Citation	Trempe, JF, Shenker, S, Kozlov, G and Gehring, K (2011) Self-association studies of the bifunctional N-acetylglucosamine-1-phosphate uridyltransferase from Escherichia coli. Protein Sci. 20:745-52
Abstract	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 demonstrated that the enzyme is in a trimer/hexamer equilibrium. Small-angle X-ray scattering studies were performed to determine the structure of the hexameric assembly and showed that two trimers assemble through their N-terminal domains. The interaction is mediated by a loop that undergoes a large conformational change in the uridyl transferase reaction, a feature that may affect the enzymatic activity of GlmU.
Links	PubMed PMC3081552 Online version:10.1002/pro.608
Keywords	Crystallography, X-Ray; Escherichia coli/enzymology; Escherichia coli Proteins/chemistry; Models, Molecular; Nucleotidyltransferases/chemistry; Protein Structure, Quaternary; Protein Structure, Tertiary; Scattering, Small Angle
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