Literature summary for 2.4.1.227 extracted from

Brown, K.; Vial, S.C.; Dedi, N.; Westcott, J.; Scally, S.; Bugg, T.D.; Charlton, P.A.; Cheetham, G.M.
Crystal structure of the Pseudomonas aeruginosa MurG:UDP-GlcNAc substrate complex (2013), Protein Pept. Lett., 20, 1002-1008.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
complex of MurG with UDP-GlcNAc, X-ray diffraction structure determination and analysis	Pseudomonas aeruginosa

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas aeruginosa	Q9HW01	-	-

Subunits

Subunits	Comment	Organism
More	structure comparison with the MurG enzyme from Escherichia coli, overview	Pseudomonas aeruginosa

Synonyms

Synonyms	Comment	Organism
MurG	-	Pseudomonas aeruginosa

General Information

General Information	Comment	Organism
additional information	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	Pseudomonas aeruginosa
physiological function	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	Pseudomonas aeruginosa

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Release 2023.1 (January 2023)