Cysteine-to-Serine Mutants Dramatically Reorder the Active Site of Human ABO(H) Blood Group B Glycosyltransferase without Affecting Activity: Structural Insights into Cooperative Substrate Binding

A common feature in the structures of GT-A-fold-type glycosyltransferases is a mobile polypeptide loop that has been observed to participate in substrate recognition and enclose the active site upon substrate binding. This is the case for the human ABO(H) blood group B glycosyltransferase GTB, where...

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Detalhes bibliográficos
Main Authors: Schuman, Brock, Persson, Mattias, Landry, Roxanne C., Polakowski, Robert, Weadge, Joel T., Seto, Nina O. L., Borisova, Svetlana N., Palcic, Monica M., Evans, Stephen V.
Formato: Artigo
Idioma:Inglês
Publicado em: 2010
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Article
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC3069981/
https://ncbi.nlm.nih.gov/pubmed/20655926
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.jmb.2010.07.036
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