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New page: left|200px<br /><applet load="1fxj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fxj, resolution 2.25Å" /> '''CRYSTAL STRUCTURE OF...
 
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[[Image:1fxj.jpg|left|200px]]<br /><applet load="1fxj" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1fxj.jpg|left|200px]]<br /><applet load="1fxj" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1fxj, resolution 2.25&Aring;" />
caption="1fxj, resolution 2.25&Aring;" />
'''CRYSTAL STRUCTURE OF N-ACETYLGLUCOSAMINE 1-PHOSPHATE URIDYLTRANSFERASE'''<br />
'''CRYSTAL STRUCTURE OF N-ACETYLGLUCOSAMINE 1-PHOSPHATE URIDYLTRANSFERASE'''<br />


==Overview==
==Overview==
N-acetylglucosamine 1-phosphate uridyltransferase (GlmU) is a cytoplasmic, bifunctional enzyme involved in the biosynthesis of the, nucleotide-activated UDP-GlcNAc, which is an essential precursor for the, biosynthetic pathways of peptidoglycan and other components in bacteria., The crystal structure of a truncated form of GlmU has been solved at 2.25, A resolution using the multiwavelength anomalous dispersion technique and, its function tested with mutagenesis studies. The molecule is composed of, two distinct domains connected by a long alpha-helical arm: (i) an, N-terminal domain which resembles the dinucleotide-binding Rossmann fold;, and (ii) a C-terminal domain which adopts a left-handed parallel, beta-helix structure (LbetaH) as found in homologous bacterial, acetyltransferases. Three GlmU molecules assemble into a trimeric, arrangement with tightly packed parallel LbetaH domains, the long, alpha-helical linkers being seated on top of the arrangement and the, N-terminal domains projected away from the 3-fold axis. In addition, the, 2.3 A resolution structure of the GlmU-UDP-GlcNAc complex reveals the, structural bases required for the uridyltransferase activity. These, structures exemplify a three-dimensional template for the development of, new antibacterial agents and for studying other members of the large, family of XDP-sugar bacterial pyrophosphorylases.
N-acetylglucosamine 1-phosphate uridyltransferase (GlmU) is a cytoplasmic bifunctional enzyme involved in the biosynthesis of the nucleotide-activated UDP-GlcNAc, which is an essential precursor for the biosynthetic pathways of peptidoglycan and other components in bacteria. The crystal structure of a truncated form of GlmU has been solved at 2.25 A resolution using the multiwavelength anomalous dispersion technique and its function tested with mutagenesis studies. The molecule is composed of two distinct domains connected by a long alpha-helical arm: (i) an N-terminal domain which resembles the dinucleotide-binding Rossmann fold; and (ii) a C-terminal domain which adopts a left-handed parallel beta-helix structure (LbetaH) as found in homologous bacterial acetyltransferases. Three GlmU molecules assemble into a trimeric arrangement with tightly packed parallel LbetaH domains, the long alpha-helical linkers being seated on top of the arrangement and the N-terminal domains projected away from the 3-fold axis. In addition, the 2.3 A resolution structure of the GlmU-UDP-GlcNAc complex reveals the structural bases required for the uridyltransferase activity. These structures exemplify a three-dimensional template for the development of new antibacterial agents and for studying other members of the large family of XDP-sugar bacterial pyrophosphorylases.


==About this Structure==
==About this Structure==
1FXJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SO4 and MES as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/UDP-N-acetylglucosamine_diphosphorylase UDP-N-acetylglucosamine diphosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.23 2.7.7.23] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FXJ OCA].  
1FXJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=MES:'>MES</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/UDP-N-acetylglucosamine_diphosphorylase UDP-N-acetylglucosamine diphosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.23 2.7.7.23] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FXJ OCA].  


==Reference==
==Reference==
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[[Category: pyrophosphorylase]]
[[Category: pyrophosphorylase]]


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