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

Authors
Olsen, LR Tian, Y Roderick, SL
Citation
Lr. Olsen et al., Purification, crystallization and preliminary X-ray data for Escherichia coli GlmU: a bifunctional acetyltransferase/uridyltransferase, ACT CRYST D, 57, 2001, pp. 296-297
Citations number
13
Categorie Soggetti
Chemistry & Analysis
Journal title
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
ISSN journal
09074449 → ACNP
Volume
57
Year of publication
2001
Part
2
Pages
296 - 297
Database
ISI
SICI code
0907-4449(200102)57:<296:PCAPXD>2.0.ZU;2-A
Abstract
Crystals of Escherichia coli GlmU, a bifunctional enzyme catalyzing the ace tylation of glucosamine-1-phosphate and uridylylation of N-acetylglucosamin e-1-phosphate to produce UDP-GlcNAc, have been prepared in complex with coe nzyme A and UDP-GlcNAc. These crystals belong to space group R32, with unit -cell parameters a = 104.5, c = 648.2 Angstrom, diffract to at least 2.1 An gstrom resolution and may contain two subunits of the trimeric enzyme per a symmetric unit.