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

Published

Journal Article (Review)

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.

Full Text

Duke Authors

Cited Authors

  • Erickson, HP

Published Date

  • February 2001

Published In

Volume / Issue

  • 13 / 1

Start / End Page

  • 55 - 60

PubMed ID

  • 11163134

Pubmed Central ID

  • 11163134

International Standard Serial Number (ISSN)

  • 0955-0674

Digital Object Identifier (DOI)

  • 10.1016/s0955-0674(00)00174-5

Language

  • eng

Conference Location

  • England