PMID:10880432
| Citation |
Mosyak, L, Zhang, Y, Glasfeld, E, Haney, S, Stahl, M, Seehra, J and Somers, WS (2000) The bacterial cell-division protein ZipA and its interaction with an FtsZ fragment revealed by X-ray crystallography. EMBO J. 19:3179-91 |
|---|---|
| Abstract |
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. |
| Links |
PubMed PMC313961 Online version:10.1093/emboj/19.13.3179 |
| Keywords |
Amino Acid Sequence; Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Carrier Proteins/chemistry; Carrier Proteins/metabolism; Cell Cycle Proteins/chemistry; Cell Cycle Proteins/metabolism; Crystallography, X-Ray; Cytoskeletal Proteins; Escherichia coli/metabolism; Escherichia coli Proteins; Models, Molecular; Molecular Sequence Data; Peptide Fragments/chemistry; Peptide Fragments/metabolism; Protein Conformation; Sequence Homology, Amino Acid |
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