Structure of a small-molecule inhibitor complexed with GlmU from Haemophilus influenzae reveals an allosteric binding site
Article first published online: 2 JAN 2009
Copyright © 2008 The Protein Society
Volume 17, Issue 3, pages 577–582, March 2008
How to Cite
Mochalkin, I., Lightle, S., Narasimhan, L., Bornemeier, D., Melnick, M., VanderRoest, S. and McDowell, L. (2008), Structure of a small-molecule inhibitor complexed with GlmU from Haemophilus influenzae reveals an allosteric binding site. Protein Science, 17: 577–582. doi: 10.1110/ps.073271408
- Issue published online: 2 JAN 2009
- Article first published online: 2 JAN 2009
- Manuscript Revised: 26 NOV 2007
- Manuscript Accepted: 26 NOV 2007
- Manuscript Received: 30 SEP 2007
- 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: 5159–5169. and
- 1999. Crystal structure of the bifunctional N-acetylglucosamine-1-phosphate uridyltransferase from Escherichia coli: A paradigm for the related pyrophosphorylase superfamily. EMBO J. 18: 4096–4107. , , , , , and
- 1998. Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D54: 905–921. , , , , , , , , , , et al.
- Collaborative Computational Project, Number 4 1994. The CCP4 Suite: Programs for protein crystallography. Acta Crystallogr. D50: 760–763.
- 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: 579–585. , , , , and
- 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: 279–289. , , , and
- 1993. PROCHECK: A program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26: 283–291. , , , and
- 1993. Identification of the glmU gene encoding N-acetylglucomsamine-1-phosphate uridyltransferase in Escherichia coli. J. Bacteriol. 175: 6150–6157. and
- 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: 5788–5795. and
- 2007. Characterization of substrate binding and catalysis in the potential antibacterial target N-acetylglucosamine-1-phosphate uridyltransferase (GlmU). Protein Sci. 16: 2657–2666. , , , , , , , , and
- 2001a. A number of real-space torsion-angle refinement techniques for proteins, nucleic acids, ligands and solvent. Acta Crystallogr. D57: 82–94.
- 2001b. X-LIGAND: An application for the automated addition of flexible ligands into electron density. Acta Crystallogr. D57: 696–705.
- 2001. Structure of the Escherichia coli GlmU pyrophosphorylase and acetyltransferase active sites. Biochemistry 40: 1913–1921. and
- 2007. Structure of the E. coli bifunctional GlmU acetyltransferase active site with substrates and products. Protein Sci. 16: 1230–1235. , , and
- 1997. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276: 307–326. and
- 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: 4799–4803. , , and
- 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: 11844–11851. , , , , and