• Anderson, M.S. and Raetz, C.R.H. 1987. Biosynthesis of lipid A precursors in Escherichia coli. A cytoplasmic acyltransferase 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.
  • Brunger, 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. D Biol. Crystallogr. 54: 905921.
  • DeLano, W.L. 2002. The PyMOL user's manual. DeLano Scientific, San Carlos, CA.
  • Dicker, I.B. and Seetharam, S. 1992. What is known about the structure and function of the Escherichia coli protein FirA? Mol. Microbiol. 6: 817823.
  • 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.
  • Jones, T.A., Zou, J.-Y., Cowan, S.W., and Kjeldgaard, M. 1991. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47: 110119.
  • 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.
  • 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.
  • 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., Tian, Y., and Roderick, S.L. 2001. Purification, crystallization and preliminary X-ray data for Escherichia coli GlmU: A bifunctional acetyltransferase/uridyltransferase. Acta Crystallogr. D Biol. Crystallogr. 57: 296297.
  • Otwinoski, Z. and Minor, W. 1997. Processing of X-ray diffraction data collected in oscillation mode. In Methods in enzymology, 276(A) ed. (eds. C.W.CarterJr and R.M.Sweet), pp. 307326. Academic Press, New York.
  • 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.
  • Raetz, C.R.H. and Roderick, S.L. 1995. A left-handed parallel β helix in the structure of UDP-N-acetylglucosamine acyltransferase. Science 270: 9971000.
  • 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.
  • Vaara, M. 1992. Eight bacterial proteins, including UDP-N-acetylglucosamine acyltransferase (LpxA) and three other transferases of Escherichia coli, consist of a six-residue periodicity theme. FEMS Microbiol. Lett. 97: 249254.