1FXJ

CRYSTAL STRUCTURE OF N-ACETYLGLUCOSAMINE 1-PHOSPHATE URIDYLTRANSFERASE

Summary for 1FXJ

• Entry DOI: 10.2210/pdb1fxj/pdb
• Related: 1FWY
• Descriptor: UDP-N-ACETYLGLUCOSAMINE PYROPHOSPHORYLASE, SULFATE ION, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, ... (4 entities in total)
• Functional Keywords: acetyltransferase, bifunctional, drug design, pyrophosphorylase, transferase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P0ACC7
• Total number of polymer chains: 2
• Total formula weight: 72735.54

Authors

Brown, K.,Pompeo, F.,Dixon, S.,Mengin-Lecreulx, D.,Cambillau, C.,Bourne, Y. (deposition date: 2000-09-26, release date: 2000-10-18, Last modification date: 2024-10-09)

Primary citation

Brown, K.,Pompeo, F.,Dixon, S.,Mengin-Lecreulx, D.,Cambillau, C.,Bourne, Y.
Crystal structure of the bifunctional N-acetylglucosamine 1-phosphate uridyltransferase from Escherichia coli: a paradigm for the related pyrophosphorylase superfamily.
EMBO J., 18:4096-4107, 1999

PubMed 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.

PubMed: 10428949
DOI: 10.1093/emboj/18.15.4096

Experimental method

X-RAY DIFFRACTION (2.25 Å)