Kostrewa, D <br/><br/>
Crystal structures of Streptococcus pneumoniae N-acetylglucosamine-1-phosphate uridyltransferase, GlmU, in apo form at 2.33 A resolution and in complex with UDP-N-acetylglucosamine and Mg(2+) at 1.96 A resolution.  [electronic resource] 

 -  Journal of molecular biology  Jan 2001 
 - 279-89 p.  digital 
<br/><br/> Publication Type: Journal Article 
<br/><br/><label>ISSN: </label>0022-2836 
<br/><br/><label>Standard No.: </label>10.1006/jmbi.2000.4296  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Amino Acid Motifs<br/>Amino Acid Sequence<br/>Apoenzymes--chemistry<br/>Binding Sites<br/>Conserved Sequence<br/>Crystallography, X-Ray<br/>Escherichia coli--enzymology<br/>Hydrogen Bonding<br/>Magnesium--metabolism<br/>Models, Molecular<br/>Nucleotidyltransferases--chemistry<br/>Protein Structure, Secondary<br/>Protein Structure, Tertiary<br/>Sequence Deletion<br/>Streptococcus pneumoniae--enzymology<br/>Structure-Activity Relationship<br/>Uridine Diphosphate N-Acetylglucosamine--metabolism