2014.06.16，我院周叢照和陳宇星教授研究組和美國UAB的吳輝教授研究組合作在Journal of Biological Chemistry上在線發(fā)表論文：Structure of a novel O-GlcNAc transferase GtfA reveals insights into the glycosylation of pneumococcal serine-rich repeat adhesins. 2014 Jun 16. pii: jbc.M114.581934.
作者：師偉偉#、江永亮#、Zhu Fan、楊益虎、邵秋燕、楊海濱、任艷敏、吳輝*、陳宇星*、周叢照*。
Abstract：Protein glycosylation catalyzed by the O-GlcNAc transferase (OGT) plays a critical role in various biological processes. In Streptococcus pneumoniae, the core enzyme GtfA and co-activator GtfB form an OGT complex to glycosylate the serine-rich repeat (SRR) of adhesin PsrP, which is involved in the infection and pathogenesis. Here we report the 2.0-? crystal structure of GtfA, revealing a β-meander add-on domain beyond the catalytic domain. It represents a novel add-on domain, which is distinct from the all-α tetratricopeptide repeats in the only two structure-known OGTs. Structural analyses combined with binding assays indicate that this add-on domain contributes to forming an active GtfA-GtfB complex and recognizing the acceptor protein. In addition, the in vitro glycosylation system enables us to map the O-linkages to the serine residues within the first SRR of PsrP. These findings suggest that fusion with an add-on domain might be a universal mechanism for diverse OGTs that recognize varying acceptor proteins/peptides.
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