The FtsZ protofilament and attachment of ZipA - structural constraints on the FtsZ power stroke

被引：46

作者：

Erickson, HP ^{[1
]}

机构：

[1] Duke Univ, Med Ctr, Dept Cell Biol, Durham, NC 27710 USA

来源：

CURRENT OPINION IN CELL BIOLOGY | 2001年 / 13卷 / 01期

关键词：

D O I：

10.1016/S0955-0674(00)00174-5

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Bacterial cell division protein FtsZ forms protofilaments in vitro that can shift from a straight to a curved conformation. The inside of the curved protofilaments, which corresponds to the carboxyl terminus, should face the center of the cell as curvature increases during constriction of the Z-ring. ZipA, a membrane-tethered division protein, binds to a highly conserved short peptide on the carboxyl terminus of FtsZ. A model is proposed here for how membrane-bound ZipA can reach around the FtsZ protofilament to bind the carboxyterminal peptide, which faces away from the membrane.

引用

页码：55 / 60

页数：6

共 28 条

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