PMID:11173485
| Citation |
Olsen, LR, Tian, Y and Roderick, SL (2001) Purification, crystallization and preliminary X-ray data for Escherichia coli GlmU: a bifunctional acetyltransferase/uridyltransferase. Acta Crystallogr. D Biol. Crystallogr. 57:296-7 |
|---|---|
| Abstract |
Crystals of Escherichia coli GlmU, a bifunctional enzyme catalyzing the acetylation of glucosamine-1-phosphate and uridylylation of N-acetylglucosamine-1-phosphate to produce UDP-GlcNAc, have been prepared in complex with coenzyme A and UDP-GlcNAc. These crystals belong to space group R32, with unit-cell parameters a = 104.5, c = 648.2 A, diffract to at least 2.1 A resolution and may contain two subunits of the trimeric enzyme per asymmetric unit. |
| Links | |
| Keywords |
Crystallization; Crystallography, X-Ray; Escherichia coli/enzymology; Macromolecular Substances; Nucleotidyltransferases/chemistry; Nucleotidyltransferases/isolation & purification; Nucleotidyltransferases/metabolism; Protein Conformation; Protein Subunits; Recombinant Proteins/chemistry; Recombinant Proteins/isolation & purification; Recombinant Proteins/metabolism; Spectrometry, Mass, Secondary Ion; Substrate Specificity |
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