1f46
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THE BACTERIAL CELL-DIVISION PROTEIN ZIPA AND ITS INTERACTION WITH AN FTSZ FRAGMENT REVEALED BY X-RAY CRYSTALLOGRAPHY
OverviewOverview
In Escherichia coli, FtsZ, a homologue of eukaryotic tubulins, and ZipA, a, membrane-anchored protein that binds to FtsZ, are two essential components, of the septal ring structure that mediates cell division. Recent data, indicate that ZipA is involved in the assembly of the ring by linking FtsZ, to the cytoplasmic membrane and that the ZipA-FtsZ interaction is mediated, by their C-terminal domains. We present the X-ray crystal structures of, the C-terminal FtsZ-binding domain of ZipA and a complex between this, domain and a C-terminal fragment of FtsZ. The ZipA domain is a, six-stranded beta-sheet packed against three alpha-helices and contains, the split beta-alpha-beta motif found in many RNA-binding proteins. The, uncovered side of the sheet incorporates a shallow hydrophobic cavity, exposed to solvent. In the complex, the 17-residue FtsZ fragment occupies, this entire cavity of ZipA and binds as an extended beta-strand followed, by alpha-helix. An alanine-scanning mutagenesis analysis of the FtsZ, fragment was also performed, which shows that only a small cluster of the, buried FtsZ side chains is critical in binding to ZipA.
About this StructureAbout this Structure
1F46 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
The bacterial cell-division protein ZipA and its interaction with an FtsZ fragment revealed by X-ray crystallography., Mosyak L, Zhang Y, Glasfeld E, Haney S, Stahl M, Seehra J, Somers WS, EMBO J. 2000 Jul 3;19(13):3179-91. PMID:10880432
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