Domain folding and flexibility of Escherichia coli FtsZ determined by tryptophan site-directed mutagenesis.

ABSTRACT: FtsZ has two domains, the amino GTPase domain with a Rossmann fold, and the carboxyl domain that resembles the chorismate mutase fold. Bioinformatics analyses suggest that the interdomain interaction is stronger than the interaction of the protofilament longitudinal interfaces. Crystal B factor analysis of FtsZ and detected conformational changes suggest a connection between these domains. The unfolding/folding characteristics of each domain of FtsZ were tested by introducing tryptophans into the flexible region of the amino (F135W) and the carboxyl (F275W and I294W) domains. As a control, the mutation F40W was introduced in a more rigid part of the amino domain. These mutants showed a native-like structure with denaturation and renaturation curves similar to wild type. However, the I294W

SUBMITTER: Diaz-Espinoza R 

PROVIDER: S-EPMC2203363 | biostudies-literature | 2007 Aug

REPOSITORIES: biostudies-literature