1nlm: Difference between revisions

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New page: left|200px<br /><applet load="1nlm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nlm, resolution 2.50Å" /> '''CRYSTAL STRUCTURE OF...
 
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[[Image:1nlm.jpg|left|200px]]<br /><applet load="1nlm" size="450" color="white" frame="true" align="right" spinBox="true"  
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caption="1nlm, resolution 2.50&Aring;" />
caption="1nlm, resolution 2.50&Aring;" />
'''CRYSTAL STRUCTURE OF MURG:GLCNAC COMPLEX'''<br />
'''CRYSTAL STRUCTURE OF MURG:GLCNAC COMPLEX'''<br />


==Overview==
==Overview==
MurG is an essential glycosyltransferase that forms the glycosidic linkage, between N-acetyl muramyl pentapeptide and N-acetyl glucosamine in the, biosynthesis of the bacterial cell wall. This enzyme is a member of a, major superfamily of NDP-glycosyltransferases for which no x-ray, structures containing intact substrates have been reported. Here we, present the 2.5-A crystal structure of Escherichia coli MurG in complex, with its donor substrate, UDP-GlcNAc. Combined with genomic analysis of, other superfamily members and site-specific mutagenesis of E. coli MurG, this structure sheds light on the molecular basis for both donor and, acceptor selectivity for the superfamily. This structural analysis, suggests that it will be possible to evolve new glycosyltransferases from, prototypical superfamily members by varying two key loops while, maintaining the overall architecture of the family and preserving key, residues.
MurG is an essential glycosyltransferase that forms the glycosidic linkage between N-acetyl muramyl pentapeptide and N-acetyl glucosamine in the biosynthesis of the bacterial cell wall. This enzyme is a member of a major superfamily of NDP-glycosyltransferases for which no x-ray structures containing intact substrates have been reported. Here we present the 2.5-A crystal structure of Escherichia coli MurG in complex with its donor substrate, UDP-GlcNAc. Combined with genomic analysis of other superfamily members and site-specific mutagenesis of E. coli MurG, this structure sheds light on the molecular basis for both donor and acceptor selectivity for the superfamily. This structural analysis suggests that it will be possible to evolve new glycosyltransferases from prototypical superfamily members by varying two key loops while maintaining the overall architecture of the family and preserving key residues.


==About this Structure==
==About this Structure==
1NLM 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 UD2 and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NLM OCA].  
1NLM 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=UD2:'>UD2</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NLM OCA].  


==Reference==
==Reference==
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[[Category: rossmann fold]]
[[Category: rossmann fold]]


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Revision as of 15:07, 21 February 2008

File:1nlm.jpg


1nlm, resolution 2.50Å

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CRYSTAL STRUCTURE OF MURG:GLCNAC COMPLEX

OverviewOverview

MurG is an essential glycosyltransferase that forms the glycosidic linkage between N-acetyl muramyl pentapeptide and N-acetyl glucosamine in the biosynthesis of the bacterial cell wall. This enzyme is a member of a major superfamily of NDP-glycosyltransferases for which no x-ray structures containing intact substrates have been reported. Here we present the 2.5-A crystal structure of Escherichia coli MurG in complex with its donor substrate, UDP-GlcNAc. Combined with genomic analysis of other superfamily members and site-specific mutagenesis of E. coli MurG, this structure sheds light on the molecular basis for both donor and acceptor selectivity for the superfamily. This structural analysis suggests that it will be possible to evolve new glycosyltransferases from prototypical superfamily members by varying two key loops while maintaining the overall architecture of the family and preserving key residues.

About this StructureAbout this Structure

1NLM is a Single protein structure of sequence from Escherichia coli with and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the MurG:UDP-GlcNAc complex reveals common structural principles of a superfamily of glycosyltransferases., Hu Y, Chen L, Ha S, Gross B, Falcone B, Walker D, Mokhtarzadeh M, Walker S, Proc Natl Acad Sci U S A. 2003 Feb 4;100(3):845-9. Epub 2003 Jan 21. PMID:12538870

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