Crystal structure of RseB and a model of its binding mode to RseA.

ABSTRACT: The bacterial envelope stress response senses stress signals in the extracytoplasmic compartment, and activates sigma(E)-dependent transcription by degrading its antisigma factor RseA. RseB, a binding partner of RseA, plays a pivotal role in regulating this response, but its molecular mechanism is not understood. We therefore determined the crystal structure of Escherichia coli RseB at a resolution of 2.4 A. RseB is composed of two domains linked by a flexible linker and forms a loosely packed dimer with two grooves on each side. This structural feature is confirmed by small-angle scattering in solution. Analysis of the binding of various RseA mutants to RseB allowed us to identify the major RseB-binding motif in RseA. These data, coupled with analysis of small-angle scattering of the RseA

SUBMITTER: Kim DY 

PROVIDER: S-EPMC1885579 | biostudies-literature | 2007 May

REPOSITORIES: biostudies-literature