Literature DB >> 11173485

Purification, crystallization and preliminary X-ray data for Escherichia coli GlmU: a bifunctional acetyltransferase/uridyltransferase.

L R Olsen 1, Y Tian, S L Roderick .   

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.

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Year:  2001        PMID: 11173485     DOI: 10.1107/s0907444900019119

Source DB:  PubMed          Journal:  Acta Crystallogr D Biol Crystallogr        ISSN: 0907-4449


  2 in total

1.  High-throughput screening identifies novel inhibitors of the acetyltransferase activity of Escherichia coli GlmU.

Authors:  Mark P Pereira; Jan E Blanchard; Cecilia Murphy; Steven L Roderick; Eric D Brown
Journal:  Antimicrob Agents Chemother       Date:  2009-04-06       Impact factor: 5.191

2.  Structure of the E. coli bifunctional GlmU acetyltransferase active site with substrates and products.

Authors:  Laurence R Olsen; Matthew W Vetting; Steven L Roderick
Journal:  Protein Sci       Date:  2007-05-01       Impact factor: 6.725

  2 in total

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