Format

Send to

Choose Destination
Curr Opin Cell Biol. 2001 Feb;13(1):55-60.

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

Author information

1
Department of Cell Biology, Box 3709, Research Drive, Duke University Medical Center, Durham, North Carolina 27710, USA. H.Erickson@cellbio.duke.edu

Abstract

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 carboxy-terminal peptide, which faces away from the membrane.

PMID:
11163134
DOI:
10.1016/s0955-0674(00)00174-5
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center