PMID:10428949
| Citation |
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. 18:4096-107 |
|---|---|
| Abstract |
N-acetylglucosamine 1-phosphate uridyltransferase (GlmU) is a cytoplasmic bifunctional enzyme involved in the biosynthesis of the nucleotide-activated UDP-GlcNAc, which is an essential precursor for the biosynthetic pathways of peptidoglycan and other components in bacteria. The crystal structure of a truncated form of GlmU has been solved at 2.25 A resolution using the multiwavelength anomalous dispersion technique and its function tested with mutagenesis studies. The molecule is composed of two distinct domains connected by a long alpha-helical arm: (i) an N-terminal domain which resembles the dinucleotide-binding Rossmann fold; and (ii) a C-terminal domain which adopts a left-handed parallel beta-helix structure (LbetaH) as found in homologous bacterial acetyltransferases. Three GlmU molecules assemble into a trimeric arrangement with tightly packed parallel LbetaH domains, the long alpha-helical linkers being seated on top of the arrangement and the N-terminal domains projected away from the 3-fold axis. In addition, the 2.3 A resolution structure of the GlmU-UDP-GlcNAc complex reveals the structural bases required for the uridyltransferase activity. These structures exemplify a three-dimensional template for the development of new antibacterial agents and for studying other members of the large family of XDP-sugar bacterial pyrophosphorylases. |
| Links |
PubMed PMC1171487 Online version:10.1093/emboj/18.15.4096 |
| Keywords |
Acetyltransferases/chemistry; Acetyltransferases/genetics; Acetyltransferases/metabolism; Amino Acid Sequence; Binding Sites; Escherichia coli/enzymology; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Nucleotidyltransferases/chemistry; Nucleotidyltransferases/genetics; Nucleotidyltransferases/metabolism; Protein Conformation; Protein Folding; Pyrophosphatases/chemistry; Sequence Homology, Amino Acid |
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