5FO3: Zapc Cell Division Regulator From E. Coli

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 2.9A 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.
PDB ID: 5FO3Download
MMDB ID: 134496
PDB Deposition Date: 2015/11/18
Updated in MMDB: 2015/12
Experimental Method:
x-ray diffraction
Resolution: 2.9  Å
Source Organism:
Similar Structures:
Biological Unit for 5FO3: dimeric; determined by author and by software (PISA)
Molecular Components in 5FO3
Label Count Molecule
Proteins (2 molecules)
Cell Division Protein Zapc(Gene symbol: zapC)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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