Enhancement of sortase A-mediated protein ligation by inducing a β-hairpin structure around the ligation site

被引：54

作者：

Yamamura, Yuichi ^{[1
]}

Hirakawa, Hidehiko ^{[1
]}

Yamaguchi, Satoshi ^{[1
]}

Nagamune, Teruyuki ^{[1
,2
]}

机构：

[1] Univ Tokyo, Sch Engn, Dept Chem & Biotechnol, Bunkyo Ku, Tokyo 1138656, Japan

[2] Univ Tokyo, Sch Engn, Dept Bioengn, Bunkyo Ku, Tokyo 1138656, Japan

来源：

CHEMICAL COMMUNICATIONS | 2011年 / 47卷 / 16期

关键词：

STAPHYLOCOCCUS-AUREUS; KINETIC MECHANISM; SURFACE-PROTEINS; TRANSPEPTIDASE; PEPTIDE; DESIGN;

D O I：

10.1039/c0cc05334a

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

A Staphylococcus aureus transpeptidase, sortase A (SrtA), catalyzes selective peptide/protein ligations that have been applied to cell imaging and protein engineering, while the ligations do not proceed to completion due to their reversibility. We successfully enhanced SrtA-mediated protein ligation through the formation of a beta-hairpin around the ligation site.

引用

页码：4742 / 4744

页数：3

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