2d7i: Difference between revisions

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[[Image:2d7i.jpg|left|200px]]
{{Seed}}
[[Image:2d7i.png|left|200px]]


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{{STRUCTURE_2d7i|  PDB=2d7i  |  SCENE=  }}  
{{STRUCTURE_2d7i|  PDB=2d7i  |  SCENE=  }}  


'''Crsytal structure of pp-GalNAc-T10 with UDP, GalNAc and Mn2+'''
===Crsytal structure of pp-GalNAc-T10 with UDP, GalNAc and Mn2+===




==Overview==
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Mucin-type O-glycans are important carbohydrate chains involved in differentiation and malignant transformation. Biosynthesis of the O-glycan is initiated by the transfer of N-acetylgalactosamine (GalNAc) which is catalyzed by UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferases (pp-GalNAc-Ts). Here we present crystal structures of the pp-GalNAc-T10 isozyme, which has specificity for glycosylated peptides, in complex with the hydrolyzed donor substrate UDP-GalNAc and in complex with GalNAc-serine. A structural comparison with uncomplexed pp-GalNAc-T1 suggests that substantial conformational changes occur in two loops near the catalytic center upon donor substrate binding, and that a distinct interdomain arrangement between the catalytic and lectin domains forms a narrow cleft for acceptor substrates. The distance between the catalytic center and the carbohydrate-binding site on the lectin beta sub-domain influences the position of GalNAc glycosylation on GalNAc-glycosylated peptide substrates. A chimeric enzyme in which the two domains of pp-GalNAc-T10 are connected by a linker from pp-GalNAc-T1 acquires activity toward non-glycosylated acceptors, identifying a potential mechanism for generating the various acceptor specificities in different isozymes to produce a wide range of O-glycans.
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{{ABSTRACT_PUBMED_16650853}}


==About this Structure==
==About this Structure==
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[[Category: Beta trefoil]]
[[Category: Beta trefoil]]
[[Category: Rossmann fold]]
[[Category: Rossmann fold]]
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