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| The EMBO Journal
(2000) 19, 3179–3191, doi:10.1093/emboj/19.13.3179 |
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| The bacterial cell-division protein ZipA and its interaction with an FtsZ fragment revealed by X-ray crystallography |
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| Lidia Mosyak, Yan Zhang, Elizabeth Glasfeld, Steve Haney, Mark Stahl, Jasbir Seehra and William S. Somers |
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Biological Chemistry, Wyeth Research, 87 Cambridge Park Drive, Cambridge, MA 02140, USA To whom correspondence should be addressed William S. Somers, wsomers@genetics.com Received 14 April 2000; Revised 17 May 2000; Accepted 18 May 2000. |
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| Abstract |
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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  -sheet packed against three  -helices and contains the split –– 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 -strand followed by -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. |
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| Keywords: bacterial cell division, crystal structure, FtsZ, single isomorphous replacement, ZipA |
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