title: Crystal structure of the Z-ring associated cell division protein ZapC from Escherichia coli.
abstract: Bacterial cell division involves a contractile ring that organises downstream proteins at the division site and which contains the tubulin homologue FtsZ. ZapC has been discovered as a non-essential regulator of FtsZ. It localises to the septal ring and deletion of zapC leads to a mild phenotype, while overexpression inhibits cell division. Interference with cell division is facilitated by an interaction with FtsZ. Here, we present the 2.9 Å crystal structure of ZapC from Escherichia coli. ZapC forms a dimer and comprises two domains that belong to the Royal superfamily of which many members bind methylated arginines or lysines. ZapC contains an N-terminal chromo-like domain and a Tudor-like C-terminal domain. We show by ITC that ZapC binds the C-terminal tail of FtsZ.
authors.affiliation: MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK; Centro Nacional de Biotecnología, CSIC C/ Darwin 3, 28049 Madrid, Spain.
authors.forename: Cristina
authors.initials: C
authors.lastname: Ortiz
authors.affiliation: MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.
authors.forename: Danguole
authors.initials: D
authors.lastname: Kureisaite-Ciziene
authors.affiliation: MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.
authors.forename: Florian
authors.initials: F
authors.lastname: Schmitz
authors.affiliation: MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.
authors.forename: Stephen H
authors.initials: SH
authors.lastname: McLaughlin
authors.affiliation: Centro Nacional de Biotecnología, CSIC C/ Darwin 3, 28049 Madrid, Spain.
authors.forename: Miguel
authors.initials: M
authors.lastname: Vicente
authors.affiliation: MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK. Electronic address: jyl@mrc-lmb.cam.ac.uk.
authors.forename: Jan
authors.initials: J
authors.lastname: Löwe
mesh_terms: D000595:Amino Acid Sequence; D018797:Cell Cycle Proteins / Q000737:chemistry* / Q000378:metabolism*; D018360:Crystallography, X-Ray; D004926:Escherichia coli; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary
chemical_list: D018797:Cell Cycle Proteins; D029968:Escherichia coli Proteins; C557498:ZapC protein, E coli
keywords: Bacterial cell division; Chromo domain; Divisome; FtsZ; Tudor domain; Z-ring