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.
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页码：55 / 60
页数：6
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