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Structural analysis of the autoinhibition of Ets-1 and its role in protein partnerships 总被引:3,自引:0,他引:3
Garvie CW Pufall MA Graves BJ Wolberger C 《The Journal of biological chemistry》2002,277(47):45529-45536
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Wei-Wei Shi Yong-Liang Jiang Fan Zhu Yi-Hu Yang Qiu-Yan Shao Hong-Bo Yang Yan-Min Ren Hui Wu Yuxing Chen Cong-Zhao Zhou 《The Journal of biological chemistry》2014,289(30):20898-20907
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 (pneumococcal serine-rich repeat protein), which is involved in the infection and pathogenesis. Here we report the 2.0 Å 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. 相似文献
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