5fo3 | pdb_00005fo3

ZapC cell division regulator from E. coli

spinqualitylabelsall models 5fo3, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5fo3 is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [ZAPC_ECOLI] Contributes to the efficiency of the cell division process by stabilizing the polymeric form of the cell division protein FtsZ. Acts by promoting interactions between FtsZ protofilaments and suppressing the GTPase activity of FtsZ.[HAMAP-Rule:MF_00906] Publication Abstract from PubMed 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. Crystal structure of the Z-ring associated cell division protein ZapC from Escherichia coli.,Ortiz C, Kureisaite-Ciziene D, Schmitz F, McLaughlin SH, Vicente M, Lowe J FEBS Lett. 2015 Nov 30. pii: S0014-5793(15)01034-0. doi:, 10.1016/j.febslet.2015.11.030. PMID:26619764 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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