Purification, crystallization and preliminary X-ray data for Escherichia coli GlmU: a bifunctional acetyltransferase/uridyltransferase.
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.
Olsen
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Department of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA.
Tian
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Y
Roderick
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SL
D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology*; D046911:Macromolecular Substances; D009713:Nucleotidyltransferases / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D011487:Protein Conformation; D021122:Protein Subunits; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D018629:Spectrometry, Mass, Secondary Ion; D013379:Substrate Specificity
D046911:Macromolecular Substances; D021122:Protein Subunits; D011994:Recombinant Proteins; D009713:Nucleotidyltransferases; C023226:UDPacetylglucosamine pyrophosphorylase