Crystal structure of the Z‐ring associated cell division protein ZapC from Escherichia coli. Issue 24 (30th November 2015)

• Record Type: Journal Article
• Authors: Ortiz, Cristina; Kureisaite-Ciziene, Danguole; Schmitz, Florian; McLaughlin, Stephen H.; Vicente, Miguel; Löwe, Jan
• Is Part Of: FEBS letters. Volume 589:Issue 24(2015) Part B
• Page Start: 3822
• Page End: 3828
• Publication Date: 2015-11-30
• Subjects: Bacterial cell division -- FtsZ -- Divisome -- Z-ring -- Tudor domain -- Chromo domain; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1016/j.febslet.2015.11.030
• Languages: English
• ISSNs: 0014-5793

Abstract

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. Abstract : First crystal structure of bacterial cell division regulator ZapC solved. ZapC is a two‐domain protein, with similarities to Tudor and chromo domains. ZapC binds the C‐terminal tail of FtsZ with moderate affinity.