1foa: Difference between revisions

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{{STRUCTURE_1foa|  PDB=1foa  |  SCENE=  }}  
{{STRUCTURE_1foa|  PDB=1foa  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF N-ACETYLGLUCOSAMINYLTRANSFERASE I'''
===CRYSTAL STRUCTURE OF N-ACETYLGLUCOSAMINYLTRANSFERASE I===




==Overview==
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N:-acetylglucosaminyltransferase I (GnT I) serves as the gateway from oligomannose to hybrid and complex N:-glycans and plays a critical role in mammalian development and possibly all metazoans. We have determined the X-ray crystal structure of the catalytic fragment of GnT I in the absence and presence of bound UDP-GlcNAc/Mn(2+) at 1.5 and 1.8 A resolution, respectively. The structures identify residues critical for substrate binding and catalysis and provide evidence for similarity, at the mechanistic level, to the deglycosylation step of retaining beta-glycosidases. The structuring of a 13 residue loop, resulting from UDP-GlcNAc/Mn(2+) binding, provides an explanation for the ordered sequential 'Bi Bi' kinetics shown by GnT I. Analysis reveals a domain shared with Bacillus subtilis glycosyltransferase SpsA, bovine beta-1,4-galactosyl transferase 1 and Escherichia coli N:-acetylglucosamine-1-phosphate uridyltransferase. The low sequence identity, conserved fold and related functional features shown by this domain define a superfamily whose members probably share a common ancestor. Sequence analysis and protein threading show that the domain is represented in proteins from several glycosyltransferase families.
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{{ABSTRACT_PUBMED_11032794}}


==About this Structure==
==About this Structure==
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[[Category: Donor substrate and metal ion complex]]
[[Category: Donor substrate and metal ion complex]]
[[Category: N-acetylglucosaminyltransferase i]]
[[Category: N-acetylglucosaminyltransferase i]]
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