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Crystal structure of the Pseudomonas aeruginosa MurG : UDP-GlcNAc substrate complex
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Brown, Kieron, Vial, Sarah C. M., Dedi, Neesha, Westcott, James, Scally, Stephen, Bugg, Tim, Charlton, Peter A. and Cheetham, Graham M. T. (2013) Crystal structure of the Pseudomonas aeruginosa MurG : UDP-GlcNAc substrate complex. Protein and Peptide Letters, Volume 20 (Number 9). pp. 1002-1008. doi:10.2174/0929866511320090006 ISSN 0929-8665.
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Official URL: http://dx.doi.org/10.2174/0929866511320090006
Abstract
MurG is an essential bacterial glycosyltransferase enzyme in Pseudomonas aeruginosa performing one of the key membrane steps of peptidoglycan synthesis catalyzing the transfer of N-acetyl glucosamine (GlcNAc) from its donor substrate, UDP-GlcNAc, to the acceptor substrate Lipid I. We have solved the crystal structure of the complex between Pseudomonas aeruginosa MurG and UDP-GlcNAc and compared it with the previously solved complex from E. coli. The structure reveals a large-scale conformational change in the relative orientations of the N- and C-terminal domains, which has the effect of widening the cofactor binding site and displacing the UDP-GlcNAc donor. These results suggest new opportunities to design potent inhibitors of peptidoglycan biosynthesis.
Item Type: | Journal Article | ||||
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Divisions: | Faculty of Science, Engineering and Medicine > Science > Chemistry | ||||
Journal or Publication Title: | Protein and Peptide Letters | ||||
Publisher: | Bentham Science Publishers Ltd. | ||||
ISSN: | 0929-8665 | ||||
Official Date: | September 2013 | ||||
Dates: |
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Volume: | Volume 20 | ||||
Number: | Number 9 | ||||
Page Range: | pp. 1002-1008 | ||||
DOI: | 10.2174/0929866511320090006 | ||||
Status: | Peer Reviewed | ||||
Publication Status: | Published | ||||
Access rights to Published version: | Restricted or Subscription Access |
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