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| {{STRUCTURE_1nlm| PDB=1nlm | SCENE= }} | | {{STRUCTURE_1nlm| PDB=1nlm | SCENE= }} |
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| '''CRYSTAL STRUCTURE OF MURG:GLCNAC COMPLEX'''
| | ===CRYSTAL STRUCTURE OF MURG:GLCNAC COMPLEX=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_12538870}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 12538870 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_12538870}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Walker, S.]] | | [[Category: Walker, S.]] |
| [[Category: Rossmann fold]] | | [[Category: Rossmann fold]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:40:39 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:28:13 2008'' |