PMID:11297730

Citation	Scheffers, DJ, de Wit, JG, den Blaauwen, T and Driessen, AJ (2001) Substitution of a conserved aspartate allows cation-induced polymerization of FtsZ. FEBS Lett. 494:34-7
Abstract	The prokaryotic tubulin homologue FtsZ polymerizes in vitro in a nucleotide dependent fashion. Here we report that replacement of the strictly conserved Asp212 residue of Escherichia coli FtsZ by a Cys or Asn, but not by a Glu residue results in FtsZ that polymerizes with divalent cations in the absence of added GTP. FtsZ D212C and D212N mutants co-purify with GTP as bound nucleotide, providing an explanation for the unusual phenotype. We conclude that D212 plays a critical role in the coordination of a metal ion and the nucleotide at the interface of two FtsZ monomers.
Links	PubMed
Keywords	Amino Acid Substitution; Aspartic Acid/genetics; Aspartic Acid/metabolism; Aspartic Acid/physiology; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Cations, Divalent; Cytoskeletal Proteins; Guanosine Triphosphate/metabolism; Mutagenesis, Site-Directed; Polymers
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