5FO3

ZapC cell division regulator from E. coli

Summary for 5FO3

• Entry DOI: 10.2210/pdb5fo3/pdb
• Descriptor: CELL DIVISION PROTEIN ZAPC (1 entity in total)
• Functional Keywords: cell cycle, ftsz, bacterial cell division, z-ring associated protein c
• Biological source: ESCHERICHIA COLI
• Cellular location: Cytoplasm : P75862
• Total number of polymer chains: 2
• Total formula weight: 42161.43

Authors

Ortiz, C.,Kureisaite-Ciziene, D.,Schmitz, F.,Vicente, M.,Lowe, J. (deposition date: 2015-11-18, release date: 2015-11-25, Last modification date: 2024-11-06)

Primary citation

Ortiz, C.,Kureisaite-Ciziene, D.,Schmitz, F.,Mclaughlin, S.H.,Vicente, M.,Lowe, J.
Crystal Structure of the Z-Ring Associated Cell Division Protein Zapc from Escherichia Coli.
FEBS Lett., 589:3822-, 2015

PubMed 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.

PubMed: 26619764
DOI: 10.1016/J.FEBSLET.2015.11.030

Experimental method

X-RAY DIFFRACTION (2.9 Å)