• Anderson, M.S. and Raetz, C.R.H. 1987. Biosynthesis of lipid A precursors in Escherichia coli. A cytoplasmic acetyltransferase that converts UDP-N-acetylglucosamine to UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine. J. Biol. Chem. 262: 51595169.
  • Brown, K., Pompeo, F., Dixon, S., Mengin-Lecreulx, D., Cambillau, C., and Bourne, Y. 1999. Crystal structure of the bifunctional N-acetylglucosamine-1-phosphate uridyltransferase from Escherichia coli: A paradigm for the related pyrophosphorylase superfamily. EMBO J. 18: 40964107.
  • Brünger, A.T., Adams, P.D., Clore, G.M., DeLano, W.L., Gros, P., Grosse-Kunstleve, R.W., Jiang, J.S., Kuszewski, J., Nilges, M., Pannu, N.S., et al. 1998. Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D54: 905921.
  • Collaborative Computational Project, Number 4 1994. The CCP4 Suite: Programs for protein crystallography. Acta Crystallogr. D50: 760763.
  • Gehring, A.M., Lees, W.J., Mindiola, D.J., Walsh, C.T., and Brown, E.D. 1996. Acetyltransfer precedes uridyltransfer in the formation of UDP-N-acetylglucosamine in separable active sites of the bifunctional glmu protein of Escherichia coli. Biochemistry 35: 579585.
  • Kostrewa, D., D'Arcy, A., Takacs, B., and Kamber, M. 2001. Crystal structure of Streptococcus pneumoniae N-acetylglucosamine-1-phosphate uridyltransferase, GlmU, in apo form at 2.33 Å resolution and in complex with UDP-N-acetylglucosamine and Mg2+ at 1.96 Å. J. Mol. Biol. 305: 279289.
  • Laskowski, R.A., MacArthur, M.W., Moss, D.S., and Thornton, J.M. 1993. PROCHECK: A program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26: 283291.
  • Mengin-Lecreulx, D. and van Heijenoort, J. 1993. Identification of the glmU gene encoding N-acetylglucomsamine-1-phosphate uridyltransferase in Escherichia coli. J. Bacteriol. 175: 61506157.
  • Mengin-Lecreulx, D. and van Heijenoort, J. 1994. Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: Characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UPD-N-acetylglucosamine synthesis. J. Bacteriol. 176: 57885795.
  • Mochalkin, I., Lightle, S., Zhu, Y., Ohren, F.Y., Spessard, C., Chirgadze, N.Y., Banotai, C., Melnick, M., and McDowell, L. 2007. Characterization of substrate binding and catalysis in the potential antibacterial target N-acetylglucosamine-1-phosphate uridyltransferase (GlmU). Protein Sci. 16: 26572666.
  • Oldfield, T.J. 2001a. A number of real-space torsion-angle refinement techniques for proteins, nucleic acids, ligands and solvent. Acta Crystallogr. D57: 8294.
  • Oldfield, T.J. 2001b. X-LIGAND: An application for the automated addition of flexible ligands into electron density. Acta Crystallogr. D57: 696705.
  • Olsen, L.R. and Roderick, S.L. 2001. Structure of the Escherichia coli GlmU pyrophosphorylase and acetyltransferase active sites. Biochemistry 40: 19131921.
  • Olsen, L.R., Vetting, M.W., and Roderick, S.L. 2007. Structure of the E. coli bifunctional GlmU acetyltransferase active site with substrates and products. Protein Sci. 16: 12301235.
  • Otwinoski, Z. and Minor, W. 1997. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276: 307326.
  • Pompeo, F., van Heijenhoort, J., and Mengin-Lecreulx, D. 1998. Probing the role of cysteine residues in glucosamine-1-phosphate acetyltransferase activity of the bifunctional glmu protein from Escherichia coli: Site-directed mutagenesis and characterization of the mutant enzymes. J. Bacteriol. 180: 47994803.
  • Sulzenbacher, G., Gal, L., Peneff, C., Fassy, F., and Bourne, Y. 2001. Crystal structure of Streptococcus pneumoniae N-acetylglucosamine-1-phosphate uridyltransferase bound to acetyl-coenzyme A reveals a novel active site architecture. J. Biol. Chem. 276: 1184411851.