The FtsZ protofilament and attachment of ZipA--structural constraints on the FtsZ power stroke.
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.
Erickson
H P
HP
Department of Cell Biology, Box 3709, Research Drive, Duke University Medical Center, Durham, North Carolina 27710, USA. H.Erickson@cellbio.duke.edu
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000502:physiology*; D002352:Carrier Proteins / Q000737:chemistry* / Q000502:physiology*; D018797:Cell Cycle Proteins / Q000737:chemistry* / Q000502:physiology*; D002455:Cell Division / Q000502:physiology; D003598:Cytoskeletal Proteins; D029968:Escherichia coli Proteins; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D013329:Structure-Activity Relationship
D001426:Bacterial Proteins; D002352:Carrier Proteins; D018797:Cell Cycle Proteins; D003598:Cytoskeletal Proteins; D029968:Escherichia coli Proteins; C071525:FtsZ protein, Bacteria; C103795:ZipA protein, E coli