期刊
PROTEIN SCIENCE
卷 20, 期 4, 页码 745-752出版社
WILEY
DOI: 10.1002/pro.608
关键词
GlmU; SAXS; AUC; self-association; beta helix
资金
- Canadian Institutes of Health Research Genomics [GSP-48370]
- CIHR
- Chercheur National of the Fonds de la recherche en sante du Quebec
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.
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